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

3VUX

Crystal structure of A20 ZF7 in complex with linear ubiquitin, form II

Functional Information from GO Data
ChainGOidnamespacecontents
E0003677molecular_functionDNA binding
E0008270molecular_functionzinc ion binding
F0003677molecular_functionDNA binding
F0008270molecular_functionzinc ion binding
G0003677molecular_functionDNA binding
G0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 101
ChainResidue
ATHR7
ATHR9
AGLU34
AHOH207
GTYR789

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 801
ChainResidue
ECYS762
ECYS767
ECYS779
ECYS782

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K E 802
ChainResidue
ECYS762
EALA764
ECYS767

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 801
ChainResidue
FCYS762
FCYS767
FCYS779
FCYS782

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K F 802
ChainResidue
FCYS762
FALA764
FCYS767

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 801
ChainResidue
GCYS762
GCYS767
GCYS779
GCYS782

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K G 802
ChainResidue
GCYS762
GALA764
GCYS767

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
ECYS762
ECYS767
ECYS779
ECYS782
FCYS762
FCYS767
FCYS779
FCYS782
GCYS762
GCYS767
GCYS779
GCYS782

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Essential for function
ChainResidueDetails
CHIS68
AHIS68
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
CSER65
ASER65
BSER65

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

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

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
BGLY76
CGLY76

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
BLYS48
CLYS11
CLYS48
ALYS11
ALYS48
BLYS11

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
BLYS27
CLYS27

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
BLYS29
CLYS29

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
BLYS33
CLYS33

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
BLYS63
CLYS63

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon