M00217
type: Enzyme
rlcp: p41
rlcp: p42
cath: Rhinovirus 14, subunit 4
cath: Jelly Rolls
cath: Thrombin, subunit H
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/-.-.-.-
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/1.-.-.-
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/3.-.-.-
cath: Alpha-Beta Plaits
cath: Mitochondrial Import Receptor Subunit Tom20; Chain A
ec: https://purl.uniprot.org/enzyme/3.4.22.29
ec: https://purl.uniprot.org/enzyme/3.6.1.15
ec: https://purl.uniprot.org/enzyme/3.4.22.28
ec: https://purl.uniprot.org/enzyme/2.7.7.48
csa: 1cqq
uniprot: P03300
uniprot: P04936
uniprot: P08292
kegg enzyme: picornain 2A
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.4.22.29
kegg pathway: Purine metabolism
kegg pathway: Thiamine metabolism
kegg cofactor: Zinc
kegg cofactor: Magnesium
kegg substrate: Protein
kegg substrate: H2O
kegg substrate: Nucleoside triphosphate
kegg substrate: RNA(n)
kegg product: Protein
kegg product: Peptide
kegg product: Nucleoside diphosphate
kegg product: Phosphate
kegg product: RNA(n)
kegg product: Diphosphate
kegg intermediate: Peptidyl-Cys-tetrahedral-intermediate (with previous peptide)
kegg intermediate: Acyl-enzyme(Peptidyl-Cys-acyl group)
kegg intermediate: Peptidyl-Cys-tetrahedral-intermediate
pdb: 2hrvA01
pdb: 2hrvB01
pdb: 1z8rA01
pdb: 2hrvA02
pdb: 2hrvB02
pdb: 1z8rA02
pdb: 1l1nA01
pdb: 1l1nB01
pdb: 1cqqA01
pdb: 1l1nA02
pdb: 1l1nB02
pdb: 1cqqA02
active site residues resources: Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites.
active site residues resources: The picornaviral 3C proteinases: cysteine nucleophiles in serine proteinase folds.
active site residues resources: P03300
active site residues resources: P04936
references: Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications.
references: Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold.
references: Analysis of putative active site residues of the poliovirus 3C protease.
references: Identification of essential amino acid residues in the functional activity of poliovirus 2A protease.
references: Cleavage specificity on synthetic peptide substrates of human rhinovirus 2 proteinase 2A.
references: Structural and mechanistic aspects of 3C proteases from the Picornavirus family.
references: Site-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: evidence of a functional relationship with trypsin-like serine proteinases.
references: Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites.
references: Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein.
references: Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases.
references: Role for poliovirus protease 2A in cap independent translation.
references: The picornaviral 3C proteinases: cysteine nucleophiles in serine proteinase folds.
references: Spectroscopic characterization of rhinoviral protease 2A: Zn is essential for the structural integrity.
references: Mutations in the poliovirus 3CD proteinase S1-specificity pocket affect substrate recognition and RNA binding.
references: Refined X-ray crystallographic structure of the poliovirus 3C gene product.
references: The yeast Saccharomyces cerevisiae as a genetic system for obtaining variants of poliovirus protease 2A.
references: Mutational analyses support a model for the HRV2 2A proteinase.
references: Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein.
references: Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes.
references: The structures of picornaviral proteinases.
references: The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis.
references: Nitric oxide inhibits dystrophin proteolysis by coxsackieviral protease 2A through S-nitrosylation: A protective mechanism against enteroviral cardiomyopathy.
references: Characterization of the active site thiol group of rhinovirus 2A proteinase.
references: Molecular epidemiology and evolution of coxsackievirus A9.
references: Activation of human rhinovirus-14 3C protease.
references: The C-terminal residues of poliovirus proteinase 2A(pro) are critical for viral RNA replication but not for cis- or trans-proteolytic cleavage.
references: The unusual catalytic triad of poliovirus protease 3C.

Rhinovirus 14, subunit 4
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/4.10.80.-

Jelly Rolls
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.60.120.-

Thrombin, subunit H
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.40.10.10
catalytic domain: index.html

Alpha-Beta Plaits
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.70.-

Mitochondrial Import Receptor Subunit Tom20; Chain A
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.20.960.-

Purine metabolism
type: KeggPathway
references: KEGG:MAP00230
ec: https://purl.uniprot.org/enzyme/3.6.1.15
ec: https://purl.uniprot.org/enzyme/2.7.7.48

Thiamine metabolism
type: KeggPathway
references: KEGG:MAP00730
ec: https://purl.uniprot.org/enzyme/3.6.1.15

Zinc
type: KeggCofactor
references: KEGG:C00038
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/3.4.22.29
compound type: heavy metal

Magnesium
type: KeggCofactor
references: KEGG:C00305
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/2.7.7.48
compound type: divalent metal (Ca2+, Mg2+)

Protein
type: KeggSubstrate
type: KeggProduct
references: KEGG:C00017
ec: https://purl.uniprot.org/enzyme/3.4.22.28
ec: https://purl.uniprot.org/enzyme/3.4.22.29
compound type: peptide/protein

H2O
type: KeggSubstrate
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/3.4.22.28
ec: https://purl.uniprot.org/enzyme/3.4.22.29
ec: https://purl.uniprot.org/enzyme/3.6.1.15
compound type: H2O

Nucleoside triphosphate
type: KeggSubstrate
references: KEGG:C00201
ec: https://purl.uniprot.org/enzyme/3.6.1.15
ec: https://purl.uniprot.org/enzyme/2.7.7.48
compound type: nucleotide

RNA(n)
type: KeggSubstrate
type: KeggProduct
label: RNA(n+1)
references: KEGG:C00046
ec: https://purl.uniprot.org/enzyme/2.7.7.48
compound type: nucleic acids

Peptide
type: KeggProduct
references: KEGG:C00012
ec: https://purl.uniprot.org/enzyme/3.4.22.28
ec: https://purl.uniprot.org/enzyme/3.4.22.29
compound type: peptide/protein

Nucleoside diphosphate
type: KeggProduct
references: KEGG:C00454
ec: https://purl.uniprot.org/enzyme/3.6.1.15
compound type: nucleotide

Phosphate
type: KeggProduct
references: KEGG:C00009
references: CHEBI:26078
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/3.6.1.15
compound type: phosphate group/phosphate ion

Diphosphate
type: KeggProduct
references: KEGG:C00013
references: CHEBI:29888
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/2.7.7.48
compound type: phosphate group/phosphate ion

Peptidyl-Cys-tetrahedral-intermediate (with previous peptide)
type: KeggIntermediate
references: KEGG:I00153
ec: https://purl.uniprot.org/enzyme/3.4.22.28

Acyl-enzyme(Peptidyl-Cys-acyl group)
type: KeggIntermediate
references: KEGG:I00154
ec: https://purl.uniprot.org/enzyme/3.4.22.28

Peptidyl-Cys-tetrahedral-intermediate
type: KeggIntermediate
references: KEGG:I00155
ec: https://purl.uniprot.org/enzyme/3.4.22.28

2hrvA01
type: Pdb
references: 2hrv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hrv
catalytic residue: HIS 18;ASP 35

2hrvB01
type: Pdb
references: 2hrv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hrv
catalytic residue: HIS 18;ASP 35

1z8rA01
type: Pdb
references: 1z8r
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1z8r
catalytic residue: HIS 21;ASP 39

2hrvA02
type: Pdb
references: 2hrv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hrv
catalytic residue: CYS 106
cofactor binding residue: CYS 52;CYS 54;CYS 112;HIS 114(Zinc binding)
main chain in catalysis: GLY 104;CYS 106

2hrvB02
type: Pdb
references: 2hrv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hrv
catalytic residue: CYS 106
cofactor binding residue: CYS 52;CYS 54;CYS 112;HIS 114(Zinc binding)
main chain in catalysis: GLY 104;CYS 106

1z8rA02
type: Pdb
references: 1z8r
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1z8r
cofactor binding residue: CYS 56;CYS 58;CYS 116;HIS 118(Zinc binding)
main chain in catalysis: GLY 108;
comment: mutant C110A

1l1nA01
type: Pdb
references: 1l1n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1l1n
catalytic residue: HIS 40;GLU 71

1l1nB01
type: Pdb
references: 1l1n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1l1n
catalytic residue: HIS 40;GLU 71

1cqqA01
type: Pdb
references: 1cqq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cqq
catalytic residue: HIS 40;GLU 71

1l1nA02
type: Pdb
references: 1l1n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1l1n
catalytic residue: CYS 147
main chain in catalysis: GLY 145;CYS 147

1l1nB02
type: Pdb
references: 1l1n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1l1n
catalytic residue: CYS 147
main chain in catalysis: GLY 145;CYS 147

1cqqA02
type: Pdb
references: 1cqq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cqq
catalytic residue: CYS 147
main chain in catalysis: GLY 145;CYS 147

Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8097606
journal: Virology
volume: 194
pages: 360-4
published year: 1993
authors:
  item: Kean KM
  item: Howell MT
  item: Grunert S
  item: Girard M
  item: Jackson RJ

The picornaviral 3C proteinases: cysteine nucleophiles in serine proteinase folds.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8520469
journal: Protein Sci
volume: 4
pages: 1439-45
published year: 1995
authors:
  item: Malcolm BA

Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3186696
journal: Proc Natl Acad Sci U S A
volume: 85
pages: 7872-6
published year: 1988
authors:
  item: Bazan JF
  item: Fletterick RJ

Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2645167
journal: FEBS Lett
volume: 243
pages: 103-14
published year: 1989
authors:
  item: Gorbalenya AE
  item: Donchenko AP
  item: Blinov VM
  item: Koonin EV

Analysis of putative active site residues of the poliovirus 3C protease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1849679
journal: Virology
volume: 181
pages: 609-19
published year: 1991
authors:
  item: Kean KM
  item: Teterina NL
  item: Marc D
  item: Girard M

Identification of essential amino acid residues in the functional activity of poliovirus 2A protease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1850921
journal: Virology
volume: 182
pages: 615-25
published year: 1991
authors:
  item: Yu SF
  item: Lloyd RE

Cleavage specificity on synthetic peptide substrates of human rhinovirus 2 proteinase 2A.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1331062
journal: J Biol Chem
volume: 267
pages: 22639-44
published year: 1992
authors:
  item: Sommergruber W
  item: Ahorn H
  item: Zophel A
  item: Maurer-Fogy I
  item: Fessl F
  item: Schnorrenberg G
  item: Liebig HD
  item: Blaas D
  item: Kuechler E
  item: Skern T

Structural and mechanistic aspects of 3C proteases from the Picornavirus family.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8320292
journal: J Chem Inf Comput Sci
volume: 33
pages: 345-9
published year: 1993
authors:
  item: Arad D
  item: Kreisberg R
  item: Shokhen M

Site-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: evidence of a functional relationship with trypsin-like serine proteinases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8386363
journal: Protein Eng
volume: 6
pages: 189-93
published year: 1993
authors:
  item: Miyashita K
  item: Kusumi M
  item: Utsumi R
  item: Katayama S
  item: Noda M
  item: Komano T
  item: Satoh N

Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7515772
journal: Cell
volume: 77
pages: 761-71
published year: 1994
authors:
  item: Matthews DA
  item: Smith WW
  item: Ferre RA
  item: Condon B
  item: Budahazi G
  item: Sisson W
  item: Villafranca JE
  item: Janson CA
  item: McElroy HE
  item: Gribskov CL
  item: et al

Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8164744
journal: Nature
volume: 369
pages: 72-6
published year: 1994
authors:
  item: Allaire M
  item: Chernaia MM
  item: Malcolm BA
  item: James MN

Role for poliovirus protease 2A in cap independent translation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8112306
journal: EMBO J
volume: 13
pages: 924-7
published year: 1994
authors:
  item: Macadam AJ
  item: Ferguson G
  item: Fleming T
  item: Stone DM
  item: Almond JW
  item: Minor PD

Spectroscopic characterization of rhinoviral protease 2A: Zn is essential for the structural integrity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8580843
journal: Protein Sci
volume: 4
pages: 2526-31
published year: 1995
authors:
  item: Voss T
  item: Meyer R
  item: Sommergruber W

Mutations in the poliovirus 3CD proteinase S1-specificity pocket affect substrate recognition and RNA binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8615011
journal: Virology
volume: 218
pages: 1-13
published year: 1996
authors:
  item: Blair WS
  item: Nguyen JH
  item: Parsley TB
  item: Semler BL

Refined X-ray crystallographic structure of the poliovirus 3C gene product.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9367789
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Mol Biol
volume: 273
pages: 1032-47
published year: 1997
authors:
  item: Mosimann SC
  item: Cherney MM
  item: Sia S
  item: Plotch S
  item: James MN

The yeast Saccharomyces cerevisiae as a genetic system for obtaining variants of poliovirus protease 2A.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9139725
journal: J Biol Chem
volume: 272
pages: 12683-91
published year: 1997
authors:
  item: Barco A
  item: Ventoso I
  item: Carrasco L

Mutational analyses support a model for the HRV2 2A proteinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9268151
journal: Virology
volume: 234
pages: 203-14
published year: 1997
authors:
  item: Sommergruber W
  item: Seipelt J
  item: Fessl F
  item: Skern T
  item: Liebig HD
  item: Casari G

Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10400760
journal: J Virol
volume: 73
pages: 6626-33
published year: 1999
authors:
  item: Sosnovtseva SA
  item: Sosnovtsev SV
  item: Green KY

Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1507-1686.
references: http://www.ncbi.nlm.nih.gov/pubmed/10500114
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04936
journal: Proc Natl Acad Sci U S A
volume: 96
pages: 11000-7
published year: 1999
authors:
  item: Matthews DA
  item: Dragovich PS
  item: Webber SE
  item: Fuhrman SA
  item: Patick AK
  item: Zalman LS
  item: Hendrickson TF
  item: Love RA
  item: Prins TJ
  item: Marakovits JT
  item: Zhou R
  item: Tikhe J
  item: Ford CE
  item: Meador JW
  item: Ferre RA
  item: Brown EL
  item: Binford SL
  item: Brothers MA
  item: DeLisle DM
  item: Worland ST

The structures of picornaviral proteinases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10507325
journal: Virus Res
volume: 62
pages: 159-68
published year: 1999
authors:
  item: Seipelt J
  item: Guarne A
  item: Bergmann E
  item: James M
  item: Sommergruber W
  item: Fita I
  item: Skern T

The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 850-991.
references: http://www.ncbi.nlm.nih.gov/pubmed/10523291
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04936
journal: EMBO J
volume: 18
pages: 5463-75
published year: 1999
authors:
  item: Petersen JF
  item: Cherney MM
  item: Liebig HD
  item: Skern T
  item: Kuechler E
  item: James MN

Nitric oxide inhibits dystrophin proteolysis by coxsackieviral protease 2A through S-nitrosylation: A protective mechanism against enteroviral cardiomyopathy.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11056105
journal: Circulation
volume: 102
pages: 2276-81
published year: 2000
authors:
  item: Badorff C
  item: Fichtlscherer B
  item: Rhoads RE
  item: Zeiher AM
  item: Muelsch A
  item: Dimmeler S
  item: Knowlton KU

Characterization of the active site thiol group of rhinovirus 2A proteinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11007981
journal: FEBS Lett
volume: 481
pages: 289-92
published year: 2000
authors:
  item: Sarkany Z
  item: Skern T
  item: Polgar L

Molecular epidemiology and evolution of coxsackievirus A9.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10769080
journal: J Gen Virol
volume: 81
pages: 1361-72
published year: 2000
authors:
  item: Santti J
  item: Harvala H
  item: Kinnunen L
  item: Hyypia T

Activation of human rhinovirus-14 3C protease.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11162821
journal: Virology
volume: 280
pages: 80-6
published year: 2001
authors:
  item: Wang QM
  item: Johnson RB

The C-terminal residues of poliovirus proteinase 2A(pro) are critical for viral RNA replication but not for cis- or trans-proteolytic cleavage.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11161279
journal: J Gen Virol
volume: 82
pages: 397-408
published year: 2001
authors:
  item: Li X
  item: Lu HH
  item: Mueller S
  item: Wimmer E

The unusual catalytic triad of poliovirus protease 3C.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12525179
journal: Biochemistry
volume: 42
pages: 516-22
published year: 2003
authors:
  item: Sarkany Z
  item: Polgar L

Mutations at KFRDI and VGK domains of enterovirus 71 3C protease affect its RNA binding and proteolytic activities.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14966374
journal: J Biomed Sci
volume: 11
pages: 239-48
published year: 2004
authors:
  item: Shih SR
  item: Chiang C
  item: Chen TC
  item: Wu CN
  item: Hsu JT
  item: Lee JC
  item: Hwang MJ
  item: Li ML
  item: Chen GW
  item: Ho MS

A norovirus protease structure provides insights into active and substrate binding site integrity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16227288
journal: J Virol
volume: 79
pages: 13685-93
published year: 2005
authors:
  item: Nakamura K
  item: Someya Y
  item: Kumasaka T
  item: Ueno G
  item: Yamamoto M
  item: Sato T
  item: Takeda N
  item: Miyamura T
  item: Tanaka N

Structure and dynamics of coxsackievirus B4 2A proteinase, an enyzme involved in the etiology of heart disease.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/16415022
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Virol
volume: 80
pages: 1451-62
published year: 2006
authors:
  item: Baxter NJ
  item: Roetzer A
  item: Liebig HD
  item: Sedelnikova SE
  item: Hounslow AM
  item: Skern T
  item: Waltho JP

picornavirus endopeptidase 2A
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

poliovirus protease 2A
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

rhinovirus protease 2A
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

2A protease
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

2A proteinase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

protease 2A
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

proteinase 2Apro
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

picornaviral 2A proteinase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

Y-G proteinase 2A
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

poliovirus proteinase 2A
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

poliovirus protease 2Apro
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

picornaviral 2A proteinase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.29

nucleoside-triphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.15

nucleoside triphosphate phosphohydrolase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.15

nucleoside-5-triphosphate phosphohydrolase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.15

nucleoside 5-triphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.15

picornain 3C
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

picornavirus endopeptidase 3C
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

poliovirus protease 3C
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

rhinovirus protease 3C
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

foot-and-mouth protease 3C
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

poliovirus proteinase 3C
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

rhinovirus proteinase 3C
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

coxsackievirus 3C proteinase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

foot-and-mouth-disease virus proteinase 3C
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

3C protease
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

3C proteinase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

cysteine proteinase 3C
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

hepatitis A virus 3C proteinase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

protease 3C
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

tomato ringspot nepovirus 3C-related protease
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.4.22.28

RNA-directed RNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

RNA nucleotidyltransferase (RNA-directed)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

RNA nucleotidyltransferase (RNA-directed)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

RNA-dependent ribonucleate nucleotidyltransferase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

3D polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

PB1 proteins
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

PB2 proteins
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

phage f2 replicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

polymerase L
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

Q-beta replicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

phage f2 replicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

ribonucleic acid replicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

ribonucleic acid-dependent ribonucleate nucleotidyltransferase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

ribonucleic acid-dependent ribonucleic acid polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

ribonucleic replicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

ribonucleic synthetase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

RNA replicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

RNA synthetase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

RNA transcriptase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

RNA-dependent ribonucleate nucleotidyltransferase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

RDRP
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

RNA-dependent RNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

RNA-dependent RNA replicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

transcriptase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.48

IntermediateAnalogue
compound: Peptidyl-Cys-tetrahedral-intermediate (with previous peptide)
pdb: 1cqqA02
ligand het code: AG7

ReferenceForCatalyticMechanism
reference index: 2
reference section: p.110

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.623-624

ReferenceForCatalyticMechanism
reference index: 9
reference section: p.763-765, p.767-769

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.1440-1441

ReferenceForCatalyticMechanism
reference index: 17
reference section: p.210

ReferenceForCatalyticMechanism
reference index: 19
reference section: p.11000-11001

ReferenceForCatalyticMechanism
reference index: 21
reference section: p.5468-5469

ReferenceForCatalyticMechanism
reference index: 30