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3EEC

X-ray structure of human ubiquitin Cd(II) adduct

Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 101
ChainResidue
AGLU64
AHIS68
AHOH107
AHOH108

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 102
ChainResidue
AMET1
AGLU16
AASP32
AHOH109

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 103
ChainResidue
AGLU18
AASP21
ALYS29
AGLU18

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CD A 104
ChainResidue
AASP58

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 105
ChainResidue
AGLU24
AASP52

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CD A 106
ChainResidue
AASP39

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD B 201
ChainResidue
BGLU64
BHIS68

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD B 202
ChainResidue
BMET1
BGLU16
BASP32
BHOH207

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD B 203
ChainResidue
BGLU18
BGLU18
BASP21
BLYS29
BHOH208
BHOH209

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CD B 204
ChainResidue
BASP58

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD B 205
ChainResidue
BGLU24
BASP52

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CD B 206
ChainResidue
BASP39

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 Residues4
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
BARG54
BARG72
AARG54
AARG72

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Essential for function
ChainResidueDetails
BHIS68
AHIS68

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
BSER65
ASER65

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
BTHR66
ATHR66

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
AGLY76
BGLY76

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
ALYS6
BLYS6

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
AGLY76
BGLY76

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
BLYS11
BLYS48
ALYS11
ALYS48

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
ALYS27
BLYS27

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
ALYS29
BLYS29

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
ALYS33
BLYS33

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
ALYS63
BLYS63

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PDB entries from 2024-04-17

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