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6H0G

Structure of the DDB1-CRBN-pomalidomide complex bound to ZNF692(ZF4)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0005634cellular_componentnucleus
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0016020cellular_componentmembrane
B0016567biological_processprotein ubiquitination
B0030177biological_processpositive regulation of Wnt signaling pathway
B0031333biological_processnegative regulation of protein-containing complex assembly
B0031334biological_processpositive regulation of protein-containing complex assembly
B0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
B0034766biological_processnegative regulation of monoatomic ion transmembrane transport
B0035641biological_processlocomotory exploration behavior
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0044325molecular_functiontransmembrane transporter binding
B0046872molecular_functionmetal ion binding
B0048471cellular_componentperinuclear region of cytoplasm
B0060173biological_processlimb development
D0003676molecular_functionnucleic acid binding
D0005634cellular_componentnucleus
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0016020cellular_componentmembrane
E0016567biological_processprotein ubiquitination
E0030177biological_processpositive regulation of Wnt signaling pathway
E0031333biological_processnegative regulation of protein-containing complex assembly
E0031334biological_processpositive regulation of protein-containing complex assembly
E0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
E0034766biological_processnegative regulation of monoatomic ion transmembrane transport
E0035641biological_processlocomotory exploration behavior
E0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
E0044325molecular_functiontransmembrane transporter binding
E0046872molecular_functionmetal ion binding
E0048471cellular_componentperinuclear region of cytoplasm
E0060173biological_processlimb development
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN B 501
ChainResidue
BCYS323
BCYS326
BCYS391
BCYS394

site_idAC2
Number of Residues10
Detailsbinding site for residue Y70 B 502
ChainResidue
BTRP386
BTRP400
BPHE402
CGLN418
CGLY423
BASN351
BPRO352
BGLU377
BHIS378
BTRP380

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN C 501
ChainResidue
CCYS419
CCYS422
CHIS435
CHIS439

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN E 501
ChainResidue
ECYS323
ECYS326
ECYS391
ECYS394

site_idAC5
Number of Residues15
Detailsbinding site for residue Y70 E 502
ChainResidue
EASN351
EPRO352
EHIS353
EGLU377
EHIS378
ESER379
ETRP380
ETRP386
ETRP400
EPHE402
FGLN418
FCYS419
FGLU420
FCYS422
FGLY423

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN F 501
ChainResidue
FCYS419
FCYS422
FHIS435
FHIS439

Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues21
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cei..CgftCrqkaslnwHqrk..H
ChainResidueDetails
CCYS419-HIS439

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues686
DetailsRegion: {"description":"WD repeat beta-propeller A"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues668
DetailsRegion: {"description":"WD repeat beta-propeller C"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues738
DetailsRegion: {"description":"Interaction with CDT1 and CUL4A","evidences":[{"source":"PubMed","id":"15448697","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9ESW0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues476
DetailsDomain: {"description":"Lon N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01123","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues216
DetailsDomain: {"description":"CULT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25108355","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TZ4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues44
DetailsZinc finger: {"description":"C2H2-type 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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