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3IVB

Structures of SPOP-Substrate Complexes: Insights into Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATH-MacroH2ASBCpep1

Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AZN4
ACYS44
AGLU47
AASP153
AHOH217
AHOH226

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
AHOH237
AHOH237
AHOH238
AGLU113
AGLU160
AGLU160

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 3
ChainResidue
AHOH12
AGLU97
AASP152
AHOH173

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 4
ChainResidue
AZN1
AHOH8
ACYS44
AASP153
AHOH218
AHOH240

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 5
ChainResidue
AGLU46
AGLU145
AHOH218
AHOH225

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 167
ChainResidue
AGLN120
ATYR123
AHOH227
MALA170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
MSER169

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
MSER172

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
MTHR177

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
MLYS166

219140

PDB entries from 2024-05-01

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