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4BOS

Structure of OTUD2 OTU domain in complex with Ubiquitin K11-linked peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
A0030433biological_processubiquitin-dependent ERAD pathway
A0101005molecular_functiondeubiquitinase activity
B0004843molecular_functioncysteine-type deubiquitinase activity
B0016579biological_processprotein deubiquitination
B0030433biological_processubiquitin-dependent ERAD pathway
B0101005molecular_functiondeubiquitinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 B 1310
ChainResidue
ATRP212
BALA156
BASP157
BASN158
BSER159
BALA160
BHIS267
BHOH2022

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 B 1311
ChainResidue
BGLY265
BHOH2068
BHOH2079
BTYR263

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 1312
ChainResidue
BGLU251
BGLU251
BGLU251

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 C 1077
ChainResidue
AHOH2047
AHOH2082
AHOH2083
CLEU71
CHOH2019

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 C 1078
ChainResidue
AALA222
CTHR7
CLEU8
CTHR9
CLEU69
CVAL70
CLEU71
CHOH2003

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 F 1014
ChainResidue
AHIS267
AARG306
AARG307
FTHR9
FGLY10
FLYS11

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
CARG54
CARG72
EARG54
EARG72

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Essential for function
ChainResidueDetails
CHIS68
EHIS68

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
ChainResidueDetails
CSER65
ESER65

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
CTHR66
ETHR66

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
CGLY76
EGLY76

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
CLYS6
ELYS6

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
CGLY76
EGLY76

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
CLYS11
CLYS48
ELYS11
ELYS48

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
CLYS27
ELYS27

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
ChainResidueDetails
CLYS29
ELYS29

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
CLYS33
ELYS33

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
CLYS63
ELYS63

222036

PDB entries from 2024-07-03

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