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

3V6C

Crystal Structure of USP2 in complex with mutated ubiquitin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 701
ChainResidue
ATHR454
ALEU455
AMET456
AASN520
APRO522
AHOH867

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
ATRP439
AHOH966
BGLY47
BLYS48
BHOH208
AARG363
AASP367
AHIS370

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 703
ChainResidue
ACYS425
ACYS428
ACYS476
ACYS479

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 101
ChainResidue
AARG349
AHOH865
BASP52
BHOH210

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon