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6B3E

Crystal structure of human CDK12/CyclinK in complex with an inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
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
D0006357biological_processregulation of transcription by RNA polymerase II
D0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue MG A 1101
ChainResidue
AASP859
AASP877

site_idAC2
Number of Residues12
Detailsbinding site for residue CJM A 1102
ChainResidue
AHIS818
AASP819
ASER863
ALEU866
AALA876
AILE733
AGLY734
AALA754
AVAL787
AGLU814
ATYR815
AMET816

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO B 301
ChainResidue
BHIS67
BTYR68
BASP69
BTHR70

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO B 302
ChainResidue
BASP69
BGLU107
BVAL157
BGLU158

site_idAC5
Number of Residues2
Detailsbinding site for residue MG C 1101
ChainResidue
CASP859
CASP877

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO C 1102
ChainResidue
CLYS756
CGLU774
CVAL787
CPHE813
CASP877
CPHE878
CCJM1103

site_idAC7
Number of Residues14
Detailsbinding site for residue CJM C 1103
ChainResidue
CILE733
CGLY734
CALA754
CVAL787
CGLU814
CTYR815
CMET816
CHIS818
CASP819
CSER863
CASN864
CLEU866
CALA876
CEDO1102

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGQVYkAkdkdtgel..........VALK
ChainResidueDetails
AILE733-LYS756

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FlHrDIKcsNILL
ChainResidueDetails
APHE855-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
AASP859
CASP859

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AILE733
ALYS756
AGLU814
CILE733
CLYS756
CGLU814

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER889
CSER889

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
ATPO893
CTPO893

223532

PDB entries from 2024-08-07

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