S00306
type: Enzyme
rlcp: p398
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/2.7.4.9
uniprot: P00572
uniprot: P23919
kegg enzyme: dTMP kinase
kegg enzyme: thymidine monophosphate kinase
kegg enzyme: thymidylate kinase
kegg enzyme: thymidylate monophosphate kinase
kegg enzyme: thymidylic acid kinase
kegg enzyme: thymidylic kinase
kegg enzyme: deoxythymidine 5'-monophosphate kinase
kegg enzyme: TMPK
kegg enzyme: thymidine 5'-monophosphate kinase
kegg pathway: Pyrimidine metabolism
kegg cofactor: Magnesium
kegg substrate: ATP
kegg substrate: dTMP
kegg product: ADP
kegg product: dTDP
pdb: 1tmkA
pdb: 1tmkB
pdb: 2tmkA
pdb: 2tmkB
pdb: 3tmkA
pdb: 3tmkB
pdb: 3tmkC
pdb: 3tmkD
pdb: 3tmkE
pdb: 3tmkF
pdb: 3tmkG
pdb: 3tmkH
pdb: 1e2dA
pdb: 1e2eA
pdb: 1e2fA
pdb: 1e2gA
pdb: 1e2qA
pdb: 1e98A
pdb: 1e99A
pdb: 1e9aA
pdb: 1e9bA
pdb: 1e9cA
pdb: 1e9dA
pdb: 1e9eA
pdb: 1e9fA
pdb: 1nmxA
pdb: 1nmyA
pdb: 1nmzA
pdb: 1nn0A
pdb: 1nn1A
pdb: 1nn3A
pdb: 1nn5A
pdb bound state: Unbound
  compound: ATP
  pdb: 1tmkA
pdb bound state: Unbound
  compound: ATP
  pdb: 1tmkB
pdb bound state: Unbound
  compound: ATP
  pdb: 2tmkA
pdb bound state: Unbound
  compound: ATP
  pdb: 2tmkB
pdb bound state: Analogue
  compound: ATP
  pdb: 3tmkA
  ligand het code: T5A(ATP)
pdb bound state: Analogue
  compound: ATP
  pdb: 3tmkB
  ligand het code: T5A(ATP)
pdb bound state: Analogue
  compound: ATP
  pdb: 3tmkC
  ligand het code: T5A(ATP)
pdb bound state: Analogue
  compound: ATP
  pdb: 3tmkD
  ligand het code: T5A(ATP)
active site residues resources: Structural basis for efficient phosphorylation of 3'-azidothymidine monophosphate by Escherichia coli thymidylate kinase.
active site residues resources: Modifying human thymidylate kinase to potentiate azidothymidine activation.
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/S00306#16
references: AZT monophosphate knocks thymidylate kinase for a loop.
references: Improving AZT efficacy.
references: The bottleneck in AZT activation.
references: Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation.
references: Failure of AZT: a molecular perspective.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/S00306#6
references: Structural basis for efficient phosphorylation of 3'-azidothymidine monophosphate by Escherichia coli thymidylate kinase.
references: Modifying human thymidylate kinase to potentiate azidothymidine activation.
references: Crystallization and preliminary X-ray analysis of the thymidylate kinase from Mycobacterium tuberculosis.
references: Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate.
references: Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP.
references: X-ray structure of TMP kinase from Mycobacterium tuberculosis complexed with TMP at 1.95 A resolution.
references: Cryophotolysis of caged compounds: a technique for trapping intermediate states in protein crystals.
references: Mycobacterium tuberculosis thymidylate kinase: structural studies of intermediates along the reaction pathway.
references: Enzymatic and structural analysis of inhibitors designed against Mycobacterium tuberculosis thymidylate kinase. New insights into the phosphoryl transfer mechanism.
comment: This enzyme, thymidylate kinase (TmpK), was very important in terms of the medicine for AIDS, azidothymidine (AZT) [1],[2],[3]. AZT is a prodrug that must be converted by cellular enzymes, such as thymidine kinase and TmpK, to the active triphosphate form [3]. According to the paper [12], the catalytic residues and magnesium binding site of the enzyme are so various and different between those from different organisms (bacteria, archaebacteria, eukaryote, and even mammal). The paper [7] mentioned that there are two types of TmpKs. Type I TmpKs stabilize the negative charge in the transition state by having the positively charged guanidinium group originating from the P-loop (yeast enzyme), whilst in the type II enzymes the guanidinium group originates from the LID region (E. coli enzyme). Usually, NMP kinases have catallytically essential residues in the LID region. Furthermore, TmpKs use only a few basic residues to interact with the transferred phosphoryl group, whereas other NMP kinases, such as adenylate kinase or uridylate kinase, use five [7]. For example, yeast TmpK appears to have the catalytic residues in the P-loop (Arg15, Lys19), whilst it lacks basic residues in its LID region [2], [6]. Moreover, the conserved arginine residue, Arg94 in yeast TmpK (Arg100 in E. coli enzyme) also appears to interact with both the gamma-phosphate of ATP and the phosphate of the nucleoside monophosphate (i.e., the transferred phosphate and the acceptor phosphate) [7]. In contrast, in the E. coli TmpK, Arg153 from the LID region and the conserved arginine, Arg100, as well as the lysine residue in the P-loop are involved in catalysis [7]. However, in the case of human TmpK, the arginine from the P-loop does not interact with the transferred phosphoryl group. Only the conserved arginine, Arg97, plays a role in catalysis, as well as the lysine from the P-loop, and acts as a clamp to bring the donor and acceptor [10]. The archaebacterial enzyme displayed very different features …

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

Pyrimidine metabolism
type: KeggPathway
references: KEGG:MAP00240

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

ATP
type: KeggSubstrate
references: KEGG:C00002
compound type: amine group
compound type: nucleotide
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

dTMP
type: KeggSubstrate
references: KEGG:C00364
compound type: amide group
compound type: nucleotide
references: CHEBI:17013
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ADP
type: KeggProduct
references: KEGG:C00008
compound type: amine group
compound type: nucleotide
references: CHEBI:16761
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

dTDP
type: KeggProduct
references: KEGG:C00363
compound type: amide group
compound type: nucleotide
references: CHEBI:18075
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1tmkA
type: Pdb
references: 1tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

1tmkB
type: Pdb
references: 1tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

2tmkA
type: Pdb
references: 2tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

2tmkB
type: Pdb
references: 2tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

3tmkA
type: Pdb
references: 3tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

3tmkB
type: Pdb
references: 3tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

3tmkC
type: Pdb
references: 3tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

3tmkD
type: Pdb
references: 3tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

3tmkE
type: Pdb
references: 3tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

3tmkF
type: Pdb
references: 3tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

3tmkG
type: Pdb
references: 3tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

3tmkH
type: Pdb
references: 3tmk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tmk
catalytic residue: LYS 18;ARG 94
cofactor binding residue: THR 19(Mg2+ binding)

1e2dA
type: Pdb
references: 1e2d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e2d
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e2eA
type: Pdb
references: 1e2e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e2e
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e2fA
type: Pdb
references: 1e2f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e2f
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e2gA
type: Pdb
references: 1e2g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e2g
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e2qA
type: Pdb
references: 1e2q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e2q
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e98A
type: Pdb
references: 1e98
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e98
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e99A
type: Pdb
references: 1e99
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e99
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e9aA
type: Pdb
references: 1e9a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e9a
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e9bA
type: Pdb
references: 1e9b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e9b
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e9cA
type: Pdb
references: 1e9c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e9c
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e9dA
type: Pdb
references: 1e9d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e9d
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e9eA
type: Pdb
references: 1e9e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e9e
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1e9fA
type: Pdb
references: 1e9f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e9f
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1nmxA
type: Pdb
references: 1nmx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nmx
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1nmyA
type: Pdb
references: 1nmy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nmy
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1nmzA
type: Pdb
references: 1nmz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nmz
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1nn0A
type: Pdb
references: 1nn0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nn0
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1nn1A
type: Pdb
references: 1nn1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nn1
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1nn3A
type: Pdb
references: 1nn3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nn3
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

1nn5A
type: Pdb
references: 1nn5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nn5
catalytic residue: LYS 19;ARG 97
cofactor binding residue: SER 20(Mg2+ binding)

AZT monophosphate knocks thymidylate kinase for a loop.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9253402
journal: Nat Struct Biol
volume: 4
pages: 595-7
published year: 1997
authors:
  item: Kenyon GL

Improving AZT efficacy.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9461164
journal: Nat Med
volume: 4
pages: 132
published year: 1998
authors:
  item: Balzarini J
  item: Degreve B
  item: De Clercq E

The bottleneck in AZT activation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9256287
journal: Nat Med
volume: 3
pages: 922-4
published year: 1997
authors:
  item: Lavie A
  item: Schlichting I
  item: Vetter IR
  item: Konrad M
  item: Reinstein J
  item: Goody RS

Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9253404
journal: Nat Struct Biol
volume: 4
pages: 601-4
published year: 1997
authors:
  item: Lavie A
  item: Vetter IR
  item: Konrad M
  item: Goody RS
  item: Reinstein J
  item: Schlichting I
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00572

Failure of AZT: a molecular perspective.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9256270
journal: Nat Med
volume: 3
pages: 836-7
published year: 1997
authors:
  item: Hazuda D
  item: Kuo L

http://ezcatdb.cbrc.jp/EzCatDB/reference/S00306#6
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9521686
journal: Biochemistry
volume: 37
pages: 3677-86
published year: 1998
authors:
  item: Lavie A
  item: Konrad M
  item: Brundiers R
  item: Goody RS
  item: Schlichting I
  item: Reinstein J
title: Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-thymidyl) pentaphosphate (TP5A) at 2.0 A resolution: implications for catalysis and AZT activation.
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00572

Structural basis for efficient phosphorylation of 3'-azidothymidine monophosphate by Escherichia coli thymidylate kinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9826650
journal: Proc Natl Acad Sci U S A
volume: 95
pages: 14045-50
published year: 1998
authors:
  item: Lavie A
  item: Ostermann N
  item: Brundiers R
  item: Goody RS
  item: Reinstein J
  item: Konrad M
  item: Schlichting I
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P37345

Modifying human thymidylate kinase to potentiate azidothymidine activation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10585390
journal: J Biol Chem
volume: 274
pages: 35289-92
published year: 1999
authors:
  item: Brundiers R
  item: Lavie A
  item: Veit T
  item: Reinstein J
  item: Schlichting I
  item: Ostermann N
  item: Goody RS
  item: Konrad M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystallization and preliminary X-ray analysis of the thymidylate kinase from Mycobacterium tuberculosis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10666613
journal: Acta Crystallogr D Biol Crystallogr
volume: 56
pages: 226-8
published year: 2000
authors:
  item: Li de la Sierra I
  item: Munier-Lehmann H
  item: Gilles AM
  item: Barzu O
  item: Delarue M

Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10873853
journal: Structure Fold Des
volume: 8
pages: 629-42
published year: 2000
authors:
  item: Ostermann N
  item: Schlichting I
  item: Brundiers R
  item: Konrad M
  item: Reinstein J
  item: Veit T
  item: Goody RS
  item: Lavie A

Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11071809
journal: J Mol Biol
volume: 304
pages: 43-53
published year: 2000
authors:
  item: Ostermann N
  item: Lavie A
  item: Padiyar S
  item: Brundiers R
  item: Veit T
  item: Reinstein J
  item: Goody RS
  item: Konrad M
  item: Schlichting I
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

X-ray structure of TMP kinase from Mycobacterium tuberculosis complexed with TMP at 1.95 A resolution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11469859
journal: J Mol Biol
volume: 311
pages: 87-100
published year: 2001
authors:
  item: Li de la Sierra I
  item: Munier-Lehmann H
  item: Gilles AM
  item: Barzu O
  item: Delarue M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Cryophotolysis of caged compounds: a technique for trapping intermediate states in protein crystals.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11914484
journal: Acta Crystallogr D Biol Crystallogr
volume: 58
pages: 607-14
published year: 2002
authors:
  item: Ursby T
  item: Weik M
  item: Fioravanti E
  item: Delarue M
  item: Goeldner M
  item: Bourgeois D
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Mycobacterium tuberculosis thymidylate kinase: structural studies of intermediates along the reaction pathway.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12662932
journal: J Mol Biol
volume: 327
pages: 1077-92
published year: 2003
authors:
  item: Fioravanti E
  item: Haouz A
  item: Ursby T
  item: Munier-Lehmann H
  item: Delarue M
  item: Bourgeois D
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Enzymatic and structural analysis of inhibitors designed against Mycobacterium tuberculosis thymidylate kinase. New insights into the phosphoryl transfer mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12454011
journal: J Biol Chem
volume: 278
pages: 4963-71
published year: 2003
authors:
  item: Haouz A
  item: Vanheusden V
  item: Munier-Lehmann H
  item: Froeyen M
  item: Herdewijn P
  item: Van Calenbergh S
  item: Delarue M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Analogue
compound: ATP
pdb: 3tmkE
ligand het code: T5A(ATP)

Analogue
compound: ATP
pdb: 3tmkF
ligand het code: T5A(ATP)

Analogue
compound: ATP
pdb: 3tmkG
ligand het code: T5A(ATP)

Analogue
compound: ATP
pdb: 3tmkH
ligand het code: T5A(ATP)

Analogue
compound: ATP
pdb: 1e2fA
ligand het code: ANP

Analogue
compound: ATP
pdb: 1e9aA
ligand het code: Z5A(ATP)

Analogue
compound: ATP
pdb: 1e9bA
ligand het code: ANP

Analogue
compound: ATP
pdb: 1e9cA
ligand het code: ANP

Analogue
compound: ATP
pdb: 1nmyA
ligand het code: ANP

Analogue
compound: ATP
pdb: 1nmzA
ligand het code: ANP

Analogue
compound: ATP
pdb: 1nn1A
ligand het code: ANP

Analogue
compound: ATP
pdb: 1nn5A
ligand het code: ANP

Analogue
compound: dTMP
pdb: 2tmkA
ligand het code: ATM

Analogue
compound: dTMP
pdb: 2tmkB
ligand het code: ATM

Analogue
compound: dTMP
pdb: 3tmkA
ligand het code: T5A(TMP)

Analogue
compound: dTMP
pdb: 3tmkB
ligand het code: T5A(TMP)

Analogue
compound: dTMP
pdb: 3tmkC
ligand het code: T5A(TMP)

Analogue
compound: dTMP
pdb: 3tmkD
ligand het code: T5A(TMP)

Analogue
compound: dTMP
pdb: 3tmkE
ligand het code: T5A(TMP)

Analogue
compound: dTMP
pdb: 3tmkF
ligand het code: T5A(TMP)

Analogue
compound: dTMP
pdb: 3tmkG
ligand het code: T5A(TMP)

Analogue
compound: dTMP
pdb: 3tmkH
ligand het code: T5A(TMP)

Analogue
compound: dTMP
pdb: 1e98A
ligand het code: ATM

Analogue
compound: dTMP
pdb: 1e99A
ligand het code: ATM

Analogue
compound: dTMP
pdb: 1e9aA
ligand het code: Z5A(ATM)

Analogue
compound: dTMP
pdb: 1e9bA
ligand het code: ATM

Analogue
compound: dTMP
pdb: 1e9dA
ligand het code: ATM

Analogue
compound: dTMP
pdb: 1nmxA
ligand het code: FDM

Analogue
compound: dTMP
pdb: 1nmyA
ligand het code: FDM

Analogue
compound: dTMP
pdb: 1nmzA
ligand het code: NYM

Analogue
compound: dTMP
pdb: 1nn0A
ligand het code: 2DT

Analogue
compound: dTMP
pdb: 1nn1A
ligand het code: 2DT

Analogue
compound: dTMP
pdb: 1nn3A
ligand het code: 2DT

Analogue
compound: dTMP
pdb: 1nn5A
ligand het code: 2DT

TransitionStateAnalogue
pdb: 1e2eA
ligand het code: AF3

ReferenceForCatalyticMechanism
reference index: 2
reference section: p.602

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.3685

ReferenceForCatalyticMechanism
reference index: 7
reference section: p.14049-14050

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.638-639, Fig.5
reference step: 3

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.97-98

ReferenceForCatalyticMechanism
reference index: 15
reference section: Fig.6