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4EKF

Structure of the Inactive Adenovirus Proteinase at 0.98 Angstrom Resolution

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_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 301
ChainResidue
AMET147
AILE150
AHOH1036
AHOH1038
AHOH1069

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04059","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8617222","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 679
ChainResidueDetails
AHIS54proton acceptor, proton donor
AGLU71electrostatic stabiliser
AGLN115electrostatic stabiliser
AGLY123nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2025-12-17

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