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6TD3

Structure of DDB1 bound to CR8-engaged CDK12-cyclinK

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 PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue RC8 B 1101
ChainResidue
AASN907
BASP817
BHIS818
BASP819
BLEU866
AARG928
AARG947
BILE733
BALA754
BPHE813
BGLU814
BTYR815
BMET816

site_idAC2
Number of Residues13
Detailsbinding site for residue RC8 E 1101
ChainResidue
DASN907
DARG928
DARG947
EILE733
EALA754
EPHE813
EGLU814
ETYR815
EMET816
EASP817
EHIS818
EASP819
ELEU866

site_idAC3
Number of Residues14
Detailsbinding site for residue RC8 H 1101
ChainResidue
GASN907
GARG928
GARG947
HILE733
HALA754
HPHE813
HGLU814
HTYR815
HMET816
HASP817
HHIS818
HASP819
HLEU866
HASP877

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 Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
BASP859
EASP859
HASP859

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
BHIS1040
EILE733
ELYS756
EGLU814
EHIS1040
HILE733
HLYS756
HGLU814
HHIS1040
BLYS756
BGLU814
BILE733

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
HSER889
BSER889
ESER889

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:24662513, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
GLYS1121
HTPO893
ETPO893
BTPO893

219869

PDB entries from 2024-05-15

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