Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4M5W

Crystal structure of the USP7/HAUSP catalytic domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 601
ChainResidue
AGLN219
AGLY275
ALYS277

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR A 602
ChainResidue
ASER290

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 603
ChainResidue
ALEU406
AHOH704
AHOH705

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 604
ChainResidue
AARG424
AHOH780

Functional Information from PROSITE/UniProt
site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLknqGAtCYMNSlLQ
ChainResidueDetails
AGLY215-GLN230

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YiLhAVlvHsGdnhg..GHY
ChainResidueDetails
ATYR448-TYR465

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:12507430, ECO:0000269|PubMed:25944111, ECO:0000305|PubMed:11923872, ECO:0000305|PubMed:15053880, ECO:0000305|PubMed:16964248, ECO:0000305|PubMed:18716620, ECO:0000305|PubMed:21745816, ECO:0000305|PubMed:22411829
ChainResidueDetails
ACYS223

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:12507430
ChainResidueDetails
AHIS464

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
AASN218electrostatic stabiliser
ACYS223nucleofuge, nucleophile, proton acceptor, proton donor
AHIS464proton acceptor, proton donor
AASP481electrostatic stabiliser

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon