Structure of PDB 2wv4 Chain A

Receptor sequence
>2wv4A (length=201) Species: 12112 (Foot-and-mouth disease virus (strain A10-61)) [Search protein sequence]
DLQKMVMGNTKPVELILDGKTVAICCATGVFGTAYLVPRHLFAEKYDKIM
LDGRAMTDSDYRVFEFEIKVKGQDMLSDAALMVLHRGNKVRDITKHFRDT
ARMKKGTPVVGVVNNADVGRLIFSGEALTYKDIVVLMDGDTMPGLFAYKA
ATRAGYAGGAVLAKDGADTFIVGTHSAGGNGVGYCSCVSRSMLQKMKAHV
D
3D structure
PDB2wv4 Insights Into Cleavage Specificity from the Crystal Structure of Foot-and-Mouth Disease Virus 3C Protease Complexed with a Peptide Substrate.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H46 D84 A163 S182
Catalytic site (residue number reindexed from 1) H40 D78 A157 S176
Enzyme Commision number 2.7.7.48: RNA-directed RNA polymerase.
3.4.22.28: picornain 3C.
3.4.22.46: L-peptidase.
3.6.1.15: nucleoside-triphosphate phosphatase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 peptide A T27 V28 A29 I30 C31 H46 E50 D123 L142 M143 D144 D146 T158 R159 A160 G161 A163 H181 S182 A183 G184 N186 Y190 T21 V22 A23 I24 C25 H40 E44 D117 L136 M137 D138 D140 T152 R153 A154 G155 A157 H175 S176 A177 G178 N180 Y184
Gene Ontology
Molecular Function
GO:0004197 cysteine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

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Biological Process
External links
PDB RCSB:2wv4, PDBe:2wv4, PDBj:2wv4
PDBsum2wv4
PubMed19883658
UniProtP03306|POLG_FMDV1 Genome polyprotein

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