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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6TXB

Crystal structure of Mindy1 mutant (P138A) in complex with Lys48 linked di-ubiquitin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A1990380molecular_functionK48-linked deubiquitinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue NA A 401
ChainResidue
AHIS351
site_idAC2
Number of Residues2
Detailsbinding site for residue NA A 402
ChainResidue
ATYR296
AHOH548
site_idAC3
Number of Residues3
Detailsbinding site for residue NA A 403
ChainResidue
AGLN149
AGLU310
ALEU311
site_idAC4
Number of Residues1
Detailsbinding site for residue CL A 404
ChainResidue
AGLU159
site_idAC5
Number of Residues1
Detailsbinding site for residue CL A 405
ChainResidue
AGLU308
site_idAC6
Number of Residues2
Detailsbinding site for residue NA D 101
ChainResidue
DLYS6
AHIS270
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 Residues6
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
DARG54
DARG72
HARG54
HARG72
LARG54
LARG72
site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Essential for function
ChainResidueDetails
DHIS68
HHIS68
LHIS68
site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
ChainResidueDetails
DSER65
HSER65
LSER65
site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
DTHR66
HTHR66
LTHR66
site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
DGLY76
HGLY76
LGLY76
site_idSWS_FT_FI6
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
DLYS6
HLYS6
LLYS6
site_idSWS_FT_FI7
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
DGLY76
HGLY76
LGLY76
site_idSWS_FT_FI8
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
DLYS11
DLYS48
HLYS11
HLYS48
LLYS11
LLYS48
site_idSWS_FT_FI9
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
DLYS27
HLYS27
LLYS27
site_idSWS_FT_FI10
Number of Residues3
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
HLYS29
LLYS29
site_idSWS_FT_FI11
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
DLYS33
HLYS33
LLYS33
site_idSWS_FT_FI12
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
DLYS63
HLYS63
LLYS63

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PDB entries from 2024-07-17

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