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4PIE

Crystal structure of human adenovirus 2 protease a substrate based nitrile inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
A0042025cellular_componenthost cell nucleus
A0044423cellular_componentvirion component
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue 3FO A 301
ChainResidue
AGLY2
AARG48
AGLY51
AGLY52
AVAL53
ATRP55
AGLN115
ASER119
ACYS122
AARG186
ASER3
ASER4
AGLU5
AGLN6
AASP26
AASN44
AALA46
AGLY47

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 302
ChainResidue
ASER76
AASP77
ALYS109
BARG306

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 303
ChainResidue
APHE73
ATYR84
APRO117
APRO165

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 304
ChainResidue
AHIS36
ACYS199
AACT305
AHOH405

site_idAC5
Number of Residues5
Detailsbinding site for residue ACT A 305
ChainResidue
APRO35
AHIS36
AGLN82
AZN304
AHOH401

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

225946

PDB entries from 2024-10-09

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