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

4PIJ

X-ray crystal structure of the K11S/K63S double mutant of ubiquitin

Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 101
ChainResidue
ATHR7
AHIS68
ALEU69
AHOH204
BGLY47
BSO4102

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 B 101
ChainResidue
BASP52
BARG54
BHOH234
BLYS27
BASP39
BARG42

site_idAC3
Number of Residues9
Detailsbinding site for residue SO4 B 102
ChainResidue
AGLN2
AGOL101
AHOH204
AHOH209
BALA46
BHIS68
BHOH201
BHOH215
BHOH232

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 B 103
ChainResidue
AARG74
BGLU51
BASP52
BHOH222
BHOH229
BHOH234

site_idAC5
Number of Residues7
Detailsbinding site for residue SO4 B 104
ChainResidue
AARG42
AGLN49
AARG72
BARG42
BGLN49
BARG72
BLEU73

site_idAC6
Number of Residues8
Detailsbinding site for residue SO4 B 105
ChainResidue
ATHR7
ATHR9
ASER11
AGLU34
BTHR7
BLEU8
BTHR9
BGLU34

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
AARG54
AARG72
BARG54
BARG72

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

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:25474007, ECO:0000269|PubMed:25527291
ChainResidueDetails
ASER65
BSER65

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

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
ASER63
BSER63

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
BSER11
BLYS48
ASER11
ALYS48

site_idSWS_FT_FI8
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_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
ALYS29
BLYS29

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
ALYS33
BLYS33

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon