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4UN0

Crystal structure of the human CDK12-cyclinK complex

Replaces:  4CJY
Functional Information from GO Data
ChainGOidnamespacecontents
A0006357biological_processregulation of transcription by RNA polymerase II
A0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
B0006357biological_processregulation of transcription by RNA polymerase II
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGQVYkAkdkdtgel..........VALK
ChainResidueDetails
CILE733-LYS756

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FlHrDIKcsNILL
ChainResidueDetails
CPHE855-LEU867

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
CASP859
DASP859

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
CILE733
CLYS756
CGLU814
DILE733
DLYS756
DGLU814

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER889
DSER889

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:24662513, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTPO893
DTPO893

219140

PDB entries from 2024-05-01

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