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2Y6E

Structure of the D1D2 domain of USP4, the conserved catalytic domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
B0004843molecular_functioncysteine-type deubiquitinase activity
B0016579biological_processprotein deubiquitination
C0004843molecular_functioncysteine-type deubiquitinase activity
C0016579biological_processprotein deubiquitination
D0004843molecular_functioncysteine-type deubiquitinase activity
D0016579biological_processprotein deubiquitination
E0004843molecular_functioncysteine-type deubiquitinase activity
E0016579biological_processprotein deubiquitination
F0004843molecular_functioncysteine-type deubiquitinase activity
F0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1000
ChainResidue
ACYS461
ACYS464
ACYS799
ACYS802

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1926
ChainResidue
BARG373
CLYS348
CARG381
AGLN391
AMET877
AGLY878
AHOH2248
AHOH2249

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1000
ChainResidue
BCYS461
BCYS464
BCYS799
BCYS802

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1000
ChainResidue
CCYS461
CCYS464
CCYS799
CCYS802

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 1925
ChainResidue
CTYR476
CTHR478

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1000
ChainResidue
DCYS461
DCYS464
DCYS799
DCYS802

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN E 1000
ChainResidue
ECYS461
ECYS464

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN F 1000
ChainResidue
FCYS461
FCYS464

Functional Information from PROSITE/UniProt
site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLgnlGNtCFMNSaLQ
ChainResidueDetails
AGLY303-GLN318

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YdLiAVsnHyGamgv..GHY
ChainResidueDetails
ATYR865-TYR882

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01035
ChainResidueDetails
ACME311
BCME311
CCME311
DCME311
ECME311
FCME311

site_idSWS_FT_FI2
Number of Residues6
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01035
ChainResidueDetails
AHIS881
BHIS881
CHIS881
DHIS881
EHIS881
FHIS881

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:25404403, ECO:0007744|PDB:2Y6E
ChainResidueDetails
ACYS461
ACYS464
ACYS799
ACYS802
BCYS461
BCYS464
BCYS799
BCYS802
CCYS461
CCYS464
CCYS799
CCYS802
DCYS461
DCYS464
DCYS799
DCYS802
ECYS461
ECYS464
ECYS799
ECYS802
FCYS461
FCYS464
FCYS799
FCYS802

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine; by PKB/AKT1 => ECO:0000269|PubMed:30514904
ChainResidueDetails
ASER445
BSER445
CSER445
DSER445
ESER445
FSER445

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PDB entries from 2024-06-12

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