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4S1Z

Crystal structure of TRABID NZF1 in complex with K29 linked di-Ubiquitin

Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 101
ChainResidue
FCYS10
FCYS13
FCYS24
FCYS27

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 101
ChainResidue
GCYS10
GCYS13
GCYS24
GCYS27

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 101
ChainResidue
HCYS13
HCYS24
HCYS27
HCYS10

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN J 101
ChainResidue
JCYS10
JCYS13
JCYS24
JCYS27

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN I 101
ChainResidue
ICYS10
ICYS13
ICYS24
ICYS27

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

site_idPS01358
Number of Residues20
DetailsZF_RANBP2_1 Zinc finger RanBP2-type signature. WaCey..CtyeNwpsaikCtmC
ChainResidueDetails
FTRP8-CYS27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues150
DetailsZN_FING: RanBP2-type 1 => ECO:0000255|PROSITE-ProRule:PRU00322
ChainResidueDetails
FGLU3-SER33
EARG72
GGLU3-SER33
HGLU3-SER33
JGLU3-SER33
IGLU3-SER33
CARG72
DARG54
DARG72
EARG54

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00322, ECO:0000269|PubMed:25752573, ECO:0007744|PDB:4S1Z
ChainResidueDetails
FCYS10
HCYS13
HCYS24
HCYS27
JCYS10
JCYS13
JCYS24
JCYS27
ICYS10
ICYS13
ICYS24
FCYS13
ICYS27
FCYS24
FCYS27
GCYS10
GCYS13
GCYS24
GCYS27
HCYS10

site_idSWS_FT_FI3
Number of Residues5
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
CSER65
DSER65
ESER65

site_idSWS_FT_FI4
Number of Residues5
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
ATHR66
BTHR66
CTHR66
DTHR66
ETHR66

site_idSWS_FT_FI5
Number of Residues5
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
AGLY76
BGLY76
CGLY76
DGLY76
EGLY76

site_idSWS_FT_FI6
Number of Residues5
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
ALYS6
BLYS6
CLYS6
DLYS6
ELYS6

site_idSWS_FT_FI7
Number of Residues10
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
EGLY76
AGLY76
BGLY76
CGLY76
DGLY76

site_idSWS_FT_FI8
Number of Residues10
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
ALYS11
ELYS48
ALYS48
BLYS11
BLYS48
CLYS11
CLYS48
DLYS11
DLYS48
ELYS11

site_idSWS_FT_FI9
Number of Residues5
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
ALYS27
BLYS27
CLYS27
DLYS27
ELYS27

site_idSWS_FT_FI10
Number of Residues5
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
DLYS29
ELYS29

site_idSWS_FT_FI11
Number of Residues5
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
ALYS33
BLYS33
CLYS33
DLYS33
ELYS33

site_idSWS_FT_FI12
Number of Residues5
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
ALYS63
BLYS63
CLYS63
DLYS63
ELYS63

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PDB entries from 2025-06-11

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