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4PQT

Insights into the mechanism of deubiquitination by JAMM deubiquitinases from co-crystal structures of enzyme with substrate and product

Functional Information from GO Data
ChainGOidnamespacecontents
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016579biological_processprotein deubiquitination
A0061578molecular_functionK63-linked deubiquitinase activity
A0070536biological_processprotein K63-linked deubiquitination
A0140492molecular_functionmetal-dependent deubiquitinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS356
ACYS397
AHIS404
AHIS406

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AGLN416
APRO417
AGLY418
AHOH608

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 101
ChainResidue
BTHR7
BLEU8
BLEU69
BVAL70
BLEU71
BHOH207
AHOH612

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01182
ChainResidueDetails
AHIS341
AHIS343
AALA354

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS356
ACYS397
AHIS404
AHIS406

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Indirect zinc-binding => ECO:0000250
ChainResidueDetails
AGLU286

224201

PDB entries from 2024-08-28

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