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8BUP

Structure of DDB1 bound to DS30-engaged CDK12-cyclin K

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0005634cellular_componentnucleus
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0006357biological_processregulation of transcription by RNA polymerase II
C0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
D0003676molecular_functionnucleic acid binding
D0005634cellular_componentnucleus
E0004672molecular_functionprotein kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
F0006357biological_processregulation of transcription by RNA polymerase II
F0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
G0003676molecular_functionnucleic acid binding
G0005634cellular_componentnucleus
H0004672molecular_functionprotein kinase activity
H0005524molecular_functionATP binding
H0006468biological_processprotein phosphorylation
I0006357biological_processregulation of transcription by RNA polymerase II
I0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGQVYkAkdkdtgel..........VALK
ChainResidueDetails
BILE733-LYS756

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FlHrDIKcsNILL
ChainResidueDetails
BPHE855-LEU867

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1029
DetailsRegion: {"description":"WD repeat beta-propeller A"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1002
DetailsRegion: {"description":"WD repeat beta-propeller C"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1107
DetailsRegion: {"description":"Interaction with CDT1 and CUL4A","evidences":[{"source":"PubMed","id":"15448697","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9ESW0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
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 Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues42
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24662513","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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