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5CRA

Structure of the SdeA DUB Domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0016579biological_processprotein deubiquitination
B0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 A 201
ChainResidue
APRO58
AHIS59
AARG60
BASP157
BHIS158

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 202
ChainResidue
BHIS158
BASP159
AARG60
ATYR90
AHOH306
BASP157

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 203
ChainResidue
AASP157
AHIS158
AASP159
BARG60
BTYR90

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 204
ChainResidue
ALEU82
ALEU113
AASN114
AMET115
AHOH301

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 205
ChainResidue
AHIS16
AALA20
AARG21
BLYS163

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 A 206
ChainResidue
ALYS84
ATHR85
ASER111

site_idAC7
Number of Residues3
Detailsbinding site for residue GVE D 101
ChainResidue
AGLU9
AHIS64
AASN114

site_idAC8
Number of Residues5
Detailsbinding site for residue SO4 B 201
ChainResidue
AASP157
AHIS158
BPRO58
BHIS59
BARG60

site_idAC9
Number of Residues4
Detailsbinding site for residue SO4 B 202
ChainResidue
ALYS163
BHIS16
BALA20
BARG21

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 B 203
ChainResidue
BLEU82
BLEU113
BASN114
BMET115

site_idAD2
Number of Residues3
Detailsbinding site for residue GVE C 101
ChainResidue
BGLU9
BHIS64
BASN114

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
DLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
DARG54
DARG72
CARG54
CARG72

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Essential for function
ChainResidueDetails
DHIS68
CHIS68

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
DSER65
CSER65

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
DTHR66
CTHR66

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
DLYS6
CLYS6

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
DLYS63
CLYS63

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
DLYS11
DLYS48
CLYS11
CLYS48

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
DLYS27
CLYS27

site_idSWS_FT_FI9
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
DLYS29
CLYS29

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
DLYS33
CLYS33

237735

PDB entries from 2025-06-18

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