S00682
type: Enzyme
rlcp: p364
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/2.7.1.74
uniprot: P27707
kegg enzyme: Deoxycytidine kinase
kegg pathway: Purine metabolism
kegg pathway: Pyrimidine metabolism
kegg cofactor: Magnesium
kegg substrate: NTP
kegg substrate: deoxycytidine
kegg product: NDP
kegg product: dCMP
pdb: 1p5zB00
pdb: 1p60A00
pdb: 1p60B00
pdb: 1p61B00
pdb: 1p62B00
pdb: 2a2zA00
pdb: 2a2zB00
pdb: 2a2zC00
pdb: 2a2zD00
pdb: 2a30A00
pdb: 2a30B00
pdb: 2a30C00
pdb: 2a30D00
pdb: 2a7qA00
pdb: 2no0A00
pdb: 2no0B00
pdb: 2no1A00
pdb: 2no1B00
pdb: 2no6A00
pdb: 2no6B00
pdb: 2no7A00
pdb: 2no7B00
pdb: 2no9A00
pdb: 2no9B00
pdb: 2noaA00
pdb: 2noaB00
pdb: 2qrnA00
pdb: 2qrnB00
pdb: 2qrnC00
pdb: 2qrnD00
pdb: 2qroA00
pdb: 2qroB00
pdb: 2qroC00
pdb: 2qroD00
pdb: 2zi3A00
pdb: 2zi3B00
pdb: 2zi4A00
pdb: 2zi5A00
pdb: 2zi5B00
pdb: 2zi5C00
pdb: 2zi5D00
pdb: 2zi6A00
pdb: 2zi6B00
pdb: 2zi6C00
pdb: 2zi6D00
pdb: 2zi7A00
pdb: 2zi7B00
pdb: 2zi9A00
pdb: 2zi9B00
pdb: 2ziaA00
pdb: 2ziaB00
pdb: 3exkA00
pdb: 3hp1A00
pdb: 3ipxA00
pdb: 3ipyA00
pdb: 3ipyB00
pdb: 3kfxA00
pdb: 3kfxB00
pdb: 3mjrA00
pdb: 3mjrB00
pdb: 3mjrC00
pdb: 3mjrD00
pdb: 3qejA00
pdb: 3qejB00
pdb: 3qenA00
pdb: 3qenB00
pdb: 3qeoA00

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.300
catalytic domain: index.html

Purine metabolism
type: KeggPathway
references: KEGG:MAP00230

Pyrimidine metabolism
type: KeggPathway
references: KEGG:MAP00240

Magnesium
type: KeggCofactor
references: KEGG:C00305
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: divalent metal (Ca2+, Mg2+)

NTP
type: KeggSubstrate
references: KEGG:C00201
compound type: nucleotide

deoxycytidine
type: KeggSubstrate
references: KEGG:C00881
references: CHEBI:15698
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amine group
compound type: nucleoside

NDP
type: KeggProduct
references: KEGG:C00454
compound type: nucleotide

dCMP
type: KeggProduct
references: KEGG:C00239
references: CHEBI:15918
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amine group
compound type: nucleotide

1p5zB00
type: Pdb
references: 1p5z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p5z
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 65-76

1p60A00
type: Pdb
references: 1p60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p60
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34

1p60B00
type: Pdb
references: 1p60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p60
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 62-77

1p61B00
type: Pdb
references: 1p61
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p61
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 65-76

1p62B00
type: Pdb
references: 1p62
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p62
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 65-76

2a2zA00
type: Pdb
references: 2a2z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a2z
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: deletion mutant 65-79

2a2zB00
type: Pdb
references: 2a2z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a2z
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: deletion mutant 65-79

2a2zC00
type: Pdb
references: 2a2z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a2z
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: deletion mutant 65-79

2a2zD00
type: Pdb
references: 2a2z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a2z
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: deletion mutant 65-79

2a30A00
type: Pdb
references: 2a30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a30
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: deletion mutant 65-79, invisible 241-245

2a30B00
type: Pdb
references: 2a30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a30
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: deletion mutant 65-79, invisible 241-245

2a30C00
type: Pdb
references: 2a30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a30
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: deletion mutant 65-79, invisible 241-245

2a30D00
type: Pdb
references: 2a30
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a30
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: deletion mutant 65-79, invisible 241-245

2a7qA00
type: Pdb
references: 2a7q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a7q
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 65-76

2no0A00
type: Pdb
references: 2no0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2no0
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S

2no0B00
type: Pdb
references: 2no0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2no0
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 65-76, 117, 243-245

2no1A00
type: Pdb
references: 2no1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2no1
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 167-168

2no1B00
type: Pdb
references: 2no1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2no1
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 64-76, 222, 243-245

2no6A00
type: Pdb
references: 2no6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2no6
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S

2no6B00
type: Pdb
references: 2no6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2no6
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 63-77, 117, 167-168, 244

2no7A00
type: Pdb
references: 2no7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2no7
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S

2no7B00
type: Pdb
references: 2no7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2no7
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 64-77, 115-117, 167-168, 243-245

2no9A00
type: Pdb
references: 2no9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2no9
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S

2no9B00
type: Pdb
references: 2no9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2no9
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 63-76

2noaA00
type: Pdb
references: 2noa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2noa
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S

2noaB00
type: Pdb
references: 2noa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2noa
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 63-77, 115-117, 166

2qrnA00
type: Pdb
references: 2qrn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qrn
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 64-76

2qrnB00
type: Pdb
references: 2qrn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qrn
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 64-76

2qrnC00
type: Pdb
references: 2qrn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qrn
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 64-76

2qrnD00
type: Pdb
references: 2qrn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qrn
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 64-76

2qroA00
type: Pdb
references: 2qro
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qro
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 64-76

2qroB00
type: Pdb
references: 2qro
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qro
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 64-76

2qroC00
type: Pdb
references: 2qro
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qro
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 64-76

2qroD00
type: Pdb
references: 2qro
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2qro
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 64-76

2zi3A00
type: Pdb
references: 2zi3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi3
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, E247A

2zi3B00
type: Pdb
references: 2zi3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi3
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, E247A, invisible 62-79, 117

2zi4A00
type: Pdb
references: 2zi4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi4
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 64-76

2zi5A00
type: Pdb
references: 2zi5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi5
catalytic residue: LYS 1034;GLU 1053;ARG 1128;ARG 1192;ARG 1194
cofactor binding residue: SER 1035;GLU 1127(Magnesium binding)
main chain in catalysis: ALA 1032;GLY 1033;LYS 1034
comment: mutant C1009S, C1045S, C1059S, C1146S, invisible 1059-1075, 1114-1118

2zi5B00
type: Pdb
references: 2zi5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi5
catalytic residue: LYS 2034;GLU 2053;ARG 2128;ARG 2192;ARG 1194
cofactor binding residue: SER 2035;GLU 2127(Magnesium binding)
main chain in catalysis: ALA 2032;GLY 2033;LYS 2034
comment: mutant C2009S, C2045S, C2059S, C2146S, invisible 2061-2072, 2117-2119, 2166-2168

2zi5C00
type: Pdb
references: 2zi5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi5
catalytic residue: LYS 3034;GLU 3053;ARG 3128;ARG 3192;ARG 3194
cofactor binding residue: SER 3035;GLU 3127(Magnesium binding)
main chain in catalysis: ALA 3032;GLY 3033;LYS 3034
comment: mutant C3009S, C3045S, C3059S, C3146S, invisible 3060-3072, 3114-3119, 3167-3169

2zi5D00
type: Pdb
references: 2zi5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi5
catalytic residue: LYS 4034;GLU 4053;ARG 4128;ARG 4192;ARG 4194
cofactor binding residue: SER 4035;GLU 4127(Magnesium binding)
main chain in catalysis: ALA 4032;GLY 4033;LYS 4034
comment: mutant C4009S, C4045S, C4059S, C4146S, invisible 4059-4076, 4117-4119, 4168-4169

2zi6A00
type: Pdb
references: 2zi6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi6
catalytic residue: LYS 1034;GLU 1053;ARG 1128;ARG 1192;ARG 1194
cofactor binding residue: SER 1035;GLU 1127(Magnesium binding)
main chain in catalysis: ALA 1032;GLY 1033;LYS 1034
comment: mutant C1009S, C1045S, C1059S, C1146S, invisible 1059-1077, 1114-1118

2zi6B00
type: Pdb
references: 2zi6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi6
catalytic residue: LYS 2034;GLU 2053;ARG 2128;ARG 2192;ARG 1194
cofactor binding residue: SER 2035;GLU 2127(Magnesium binding)
main chain in catalysis: ALA 2032;GLY 2033;LYS 2034
comment: mutant C2009S, C2045S, C2059S, C2146S, invisible 2062-2071, 2117-2119, 2166-2168

2zi6C00
type: Pdb
references: 2zi6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi6
catalytic residue: LYS 3034;GLU 3053;ARG 3128;ARG 3192;ARG 3194
cofactor binding residue: SER 3035;GLU 3127(Magnesium binding)
main chain in catalysis: ALA 3032;GLY 3033;LYS 3034
comment: mutant C3009S, C3045S, C3059S, C3146S, invisible 3060-3075, 3114-3119, 3167-3169

2zi6D00
type: Pdb
references: 2zi6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi6
catalytic residue: LYS 4034;GLU 4053;ARG 4128;ARG 4192;ARG 4194
cofactor binding residue: SER 4035;GLU 4127(Magnesium binding)
main chain in catalysis: ALA 4032;GLY 4033;LYS 4034
comment: mutant C4009S, C4045S, C4059S, C4146S, invisible 4059-4076, 4117-4119, 4168-4169

2zi7A00
type: Pdb
references: 2zi7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi7
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 65-77, 222-230

2zi7B00
type: Pdb
references: 2zi7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi7
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 62-77, 114-120, 221-230

2zi9A00
type: Pdb
references: 2zi9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi9
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S

2zi9B00
type: Pdb
references: 2zi9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zi9
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 63-76

2ziaA00
type: Pdb
references: 2zia
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zia
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 62-77, 114-118

2ziaB00
type: Pdb
references: 2zia
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2zia
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 65-77, 114-115, 224-226

3exkA00
type: Pdb
references: 3exk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3exk
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant R104M, D133A, invisible 63-77

3hp1A00
type: Pdb
references: 3hp1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hp1
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant R104M, D133A, invisible 63-77

3ipxA00
type: Pdb
references: 3ipx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ipx
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 65-76

3ipyA00
type: Pdb
references: 3ipy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ipy
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 61-76

3ipyB00
type: Pdb
references: 3ipy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ipy
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: invisible 61-76

3kfxA00
type: Pdb
references: 3kfx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3kfx
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 65-76

3kfxB00
type: Pdb
references: 3kfx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3kfx
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S

3mjrA00
type: Pdb
references: 3mjr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3mjr
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 61-70, 168

3mjrB00
type: Pdb
references: 3mjr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3mjr
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 61-74, 167

3mjrC00
type: Pdb
references: 3mjr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3mjr
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 60-73, 167-170

3mjrD00
type: Pdb
references: 3mjr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3mjr
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 59-76, 168

3qejA00
type: Pdb
references: 3qej
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qej
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 62-69

3qejB00
type: Pdb
references: 3qej
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qej
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 63-70

3qenA00
type: Pdb
references: 3qen
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qen
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 64-69

3qenB00
type: Pdb
references: 3qen
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qen
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 63-70

3qeoA00
type: Pdb
references: 3qeo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qeo
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 62-69

3qeoB00
type: Pdb
references: 3qeo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3qeo
catalytic residue: LYS 34;GLU 53;ARG 128;ARG 192;ARG 194
cofactor binding residue: SER 35;GLU 127(Magnesium binding)
main chain in catalysis: ALA 32;GLY 33;LYS 34
comment: mutant C9S, C45S, C59S, C146S, invisible 63-70

Analogue
compound: deoxycytidine
pdb: 1p5zB00
ligand het code: AR3

Analogue
compound: deoxycytidine
pdb: 1p62B00
ligand het code: GEO

Analogue
compound: deoxycytidine
pdb: 2a7qA00
ligand het code: CFB

Analogue
compound: deoxycytidine
pdb: 2no0A00
ligand het code: GEO

Analogue
compound: deoxycytidine
pdb: 2no0B00
ligand het code: GEO

Analogue
compound: deoxycytidine
pdb: 2no6A00
ligand het code: ETV

Analogue
compound: deoxycytidine
pdb: 2no6B00
ligand het code: ETV

Analogue
compound: deoxycytidine
pdb: 2no7A00
ligand het code: LDC

Analogue
compound: deoxycytidine
pdb: 2no7B00
ligand het code: LDC

Analogue
compound: deoxycytidine
pdb: 2no9A00
ligand het code: LTT

Analogue
compound: deoxycytidine
pdb: 2no9B00
ligand het code: LTT

Analogue
compound: deoxycytidine
pdb: 2noaA00
ligand het code: 3TC

Analogue
compound: deoxycytidine
pdb: 2noaB00
ligand het code: 3TC

Analogue
compound: deoxycytidine
pdb: 2zi3A00
ligand het code: 3D1

Analogue
compound: deoxycytidine
pdb: 2zi3B00
ligand het code: 3D1

Analogue
compound: deoxycytidine
pdb: 2zi4A00
ligand het code: 3L1

Analogue
compound: deoxycytidine
pdb: 2zi5A00
ligand het code: 3L1

Analogue
compound: deoxycytidine
pdb: 2zi5B00
ligand het code: 3L1

Analogue
compound: deoxycytidine
pdb: 2zi5C00
ligand het code: 3L1

Analogue
compound: deoxycytidine
pdb: 2zi5D00
ligand het code: 3L1

Analogue
compound: deoxycytidine
pdb: 2zi6A00
ligand het code: 3D1

Analogue
compound: deoxycytidine
pdb: 2zi6B00
ligand het code: 3D1

Analogue
compound: deoxycytidine
pdb: 2zi6C00
ligand het code: 3D1

Analogue
compound: deoxycytidine
pdb: 2zi6D00
ligand het code: 3D1

Analogue
compound: deoxycytidine
pdb: 2zi7A00
ligand het code: GNG

Analogue
compound: deoxycytidine
pdb: 2zi7B00
ligand het code: GNG

Analogue
compound: deoxycytidine
pdb: 2zi9A00
ligand het code: CL9

Analogue
compound: deoxycytidine
pdb: 2zi9B00
ligand het code: CL9

Analogue
compound: deoxycytidine
pdb: 2ziaA00
ligand het code: CL9

Analogue
compound: deoxycytidine
pdb: 2ziaB00
ligand het code: CL9

Analogue
compound: deoxycytidine
pdb: 3exkA00
ligand het code: THM

Analogue
compound: deoxycytidine
pdb: 3hp1A00
ligand het code: LLT

Analogue
compound: deoxycytidine
pdb: 3ipxA00
ligand het code: B86

Analogue
compound: deoxycytidine
pdb: 3kfxA00
ligand het code: MCY

Analogue
compound: deoxycytidine
pdb: 3kfxB00
ligand het code: MCY

Analogue
compound: deoxycytidine
pdb: 3mjrA00
ligand het code: AC2

Analogue
compound: deoxycytidine
pdb: 3mjrB00
ligand het code: AC2

Analogue
compound: deoxycytidine
pdb: 3mjrD00
ligand het code: AC2

Analogue
compound: deoxycytidine
pdb: 3qenA00
ligand het code: 5BT

Analogue
compound: deoxycytidine
pdb: 3qenB00
ligand het code: 5BT

Analogue
compound: deoxycytidine
pdb: 3qeoA00
ligand het code: LLT

Analogue
compound: deoxycytidine
pdb: 3qeoB00
ligand het code: LLT

Analogue
compound: dCMP
pdb: 2qroA00
ligand het code: D5M

Analogue
compound: dCMP
pdb: 2qroB00
ligand het code: D5M

Analogue
compound: dCMP
pdb: 2qroC00
ligand het code: D5M

Analogue
compound: dCMP
pdb: 2qroD00
ligand het code: D5M

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.3, p.514-517

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.137-138

ReferenceForCatalyticMechanism
reference index: 9
reference section: Fig.5

Structural basis for substrate specificities of cellular deoxyribonucleoside kinases. Nat Struct Biol.
type: BibliographicResource
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journal: Nat Struct Bio
volume: 8
pages: 616-20
published year: 2001
authors:
  item: Johansson K
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  item: Eklund H

Kinetic analysis of human deoxycytidine kinase with the true phosphate donor uridine triphosphate.
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pages: 7540-7
published year: 1997
authors:
  item: Hughes TL
  item: Hahn TM
  item: Reynolds KK
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Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate.
type: BibliographicResource
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references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Structure
volume: 8
pages: 629-42
published year: 2000
authors:
  item: Ostermann N
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  item: Brundiers R
  item: Konrad M
  item: Reinstein J
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Structure and function of cellular deoxyribonucleoside kinases
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12363036
journal: Cell Mol Life Sci
volume: 59
pages: 1327-46
published year: 2002
authors:
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Structure of human dCK suggests strategies to improve anticancer and antiviral therapy.
type: BibliographicResource
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references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P27707
journal: Nat Struct Biol
volume: 10
pages: 513-9
published year: 2003
authors:
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The structure of human deoxycytidine kinase in complex with clofarabine reveals key interactions for prodrug activation.
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references: http://www.ncbi.nlm.nih.gov/pubmed/16421443
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Acta Crystallogr D Biol Crystallogr
volume: 62
pages: 133-9
published year: 2006
authors:
  item: Zhang Y
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  item: Ealick SE

Structural basis for the preference of UTP over ATP in human deoxycytidine kinase: illuminating the role of main-chain reorganization.
type: BibliographicResource
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references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Biochemistry
volume: 45
pages: 452-61
published year: 2006
authors:
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Structures of human deoxycytidine kinase product complexes.
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references: http://www.ncbi.nlm.nih.gov/pubmed/18084067
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Acta Crystallogr D Biol Crystallogr
volume: 63
pages: 1201-7
published year: 2007
authors:
  item: Soriano EV
  item: Clark VC
  item: Ealick SE

Nonenantioselectivity property of human deoxycytidine kinase explained by structures of the enzyme in complex with L- and D-nucleosides.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/17530837
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Med Chem
volume: 50
pages: 3004-14
published year: 2007
authors:
  item: Sabini E
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  item: Lavie A

Structural basis for activation of the therapeutic L-nucleoside analogs 3TC and troxacitabine by human deoxycytidine kinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/17158155
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journal: Nucleic Acids Res
volume: 35
pages: 186-92
published year: 2007
authors:
  item: Sabini E
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Elucidation of different binding modes of purine nucleosides to human deoxycytidine kinase.
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journal: J Med Chem
volume: 51
pages: 4219-25
published year: 2008
authors:
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Structural basis for substrate promiscuity of dCK.
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journal: J Mol Biol
volume: 378
pages: 607-21
published year: 2008
authors:
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Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase.
type: BibliographicResource
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journal: Biochemistry
volume: 48
pages: 1256-63
published year: 2009
authors:
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Lead optimization and structure-based design of potent and bioavailable deoxycytidine kinase inhibitors.
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references: http://www.ncbi.nlm.nih.gov/pubmed/19836232
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journal: Bioorg Med Chem Lett
volume: 19
pages: 6784-7
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authors:
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Structural and kinetic characterization of human deoxycytidine kinase variants able to phosphorylate 5-substituted deoxycytidine and thymidine analogues .
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http://ezcatdb.cbrc.jp/EzCatDB/reference/S00682#16
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journal: J Med Chem
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pages: 5792-800
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  item: Hazra S
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title: The sugar ring of the nucleoside is required for productive substrate positioning in the active site of human deoxycytidine kinase (dCK): implications for the development of dCK-activated acyclic guanine analogues.

Post-translational phosphorylation of serine 74 of human deoxycytidine kinase favors the enzyme adopting the open conformation making it competent for nucleoside binding and release.
type: BibliographicResource
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journal: Biochemistry
volume: 50
pages: 2870-80
published year: 2011
authors:
  item: Hazra S
  item: Szewczak A
  item: Ort S
  item: Konrad M
  item: Lavie A

Deoxycytidine kinase (phosphorylating)
type: KeggEnzyme

2'-Deoxycytidine kinase
type: KeggEnzyme

Ara-C kinase
type: KeggEnzyme

Arabinofuranosylcytosine kinase
type: KeggEnzyme

Deoxycytidine-cytidine kinase
type: KeggEnzyme