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3V6E

Crystal Structure of USP2 and a mutant form of Ubiquitin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 700
ChainResidue
ACYS425
ACYS428
ACYS476
ACYS479

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 701
ChainResidue
AHOH83
ALEU455
AMET456
AASN520
APRO522

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 702
ChainResidue
AARG349
BASP52
BHOH75

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1
ChainResidue
AHOH21
AARG363
AASP367
AHIS370
ATRP439
BGLY47
BLYS48

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

site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLrnlGNtCFMNSiLQ
ChainResidueDetails
AGLY268-GLN283

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YnLyAVsnHsGttmg..GHY
ChainResidueDetails
ATYR541-TYR558

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
BSER0

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
BSER0

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905103
ChainResidueDetails
ACYS425
ACYS428
ACYS476
ACYS479

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PDB entries from 2025-06-11

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