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3VUY

Crystal structure of A20 ZF7 in complex with linear tetraubiquitin

Functional Information from GO Data
ChainGOidnamespacecontents
D0003677molecular_functionDNA binding
D0008270molecular_functionzinc ion binding
E0003677molecular_functionDNA binding
E0008270molecular_functionzinc ion binding
F0003677molecular_functionDNA binding
F0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 801
ChainResidue
DCYS762
DCYS767
DCYS779
DCYS782

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K D 802
ChainResidue
DCYS762
DALA764
DCYS767

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 801
ChainResidue
FCYS779
FCYS782
FCYS762
FCYS767

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K F 802
ChainResidue
FCYS762
FALA764
FCYS767

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 801
ChainResidue
ECYS762
ECYS767
ECYS779
ECYS782

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K E 802
ChainResidue
ECYS762
EALA764
ECYS767

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
ALYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
ChainResidueDetails
DCYS762
ECYS767
ECYS779
ECYS782
DCYS767
DCYS779
DCYS782
FCYS762
FCYS767
FCYS779
FCYS782
ECYS762

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Essential for function
ChainResidueDetails
AHIS68
CHIS68
BHIS68

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
ASER65
CSER65
BSER65

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
ATHR66
CTHR66
BTHR66

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
AGLY76
CGLY76
BGLY76

site_idSWS_FT_FI6
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
ALYS6
CLYS6
BLYS6

site_idSWS_FT_FI7
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
AGLY76
CGLY76
BGLY76

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
ALYS11
ALYS48
CLYS11
CLYS48
BLYS11
BLYS48

site_idSWS_FT_FI9
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
ALYS27
CLYS27
BLYS27

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
ALYS29
CLYS29
BLYS29

site_idSWS_FT_FI11
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
ALYS33
CLYS33
BLYS33

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
ALYS63
CLYS63
BLYS63

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PDB entries from 2024-04-24

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