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1AVP

STRUCTURE OF HUMAN ADENOVIRUS 2 PROTEINASE WITH ITS 11 AMINO ACID COFACTOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0042025cellular_componenthost cell nucleus
A0044423cellular_componentvirion component
Functional Information from PDB Data
site_idACT
Number of Residues3
Details
ChainResidue
AHIS54
ACYS122
AGLU71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_04059, ECO:0000269|PubMed:8617222
ChainResidueDetails
AHIS54
AGLU71
ACYS122

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000255|HAMAP-Rule:MF_04059
ChainResidueDetails
AGLY51

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 679
ChainResidueDetails
AHIS54proton acceptor, proton donor
AGLU71electrostatic stabiliser
AGLN115electrostatic stabiliser
ACYS122nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-04-24

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