Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6GZH

Crystal Structure of Human CDK9/cyclinT1 with A86

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0000079biological_processregulation of cyclin-dependent protein serine/threonine kinase activity
B0000976molecular_functiontranscription cis-regulatory region binding
B0003677molecular_functionDNA binding
B0003682molecular_functionchromatin binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005829cellular_componentcytosol
B0006357biological_processregulation of transcription by RNA polymerase II
B0006366biological_processtranscription by RNA polymerase II
B0008024cellular_componentcyclin/CDK positive transcription elongation factor complex
B0009410biological_processresponse to xenobiotic stimulus
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
B0017069molecular_functionsnRNA binding
B0019901molecular_functionprotein kinase binding
B0032786biological_processpositive regulation of DNA-templated transcription, elongation
B0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
B0043923biological_processhost-mediated activation of viral transcription
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0051301biological_processcell division
B0061575molecular_functioncyclin-dependent protein serine/threonine kinase activator activity
B0070063molecular_functionRNA polymerase binding
B0070691cellular_componentP-TEFb complex
B0097322molecular_function7SK snRNA binding
B0140297molecular_functionDNA-binding transcription factor binding
B0140693molecular_functionmolecular condensate scaffold activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue LCI A 2001
ChainResidue
AILE25
AGLU107
AASP109
ALEU156
AHOH2107
AHOH2122
AGLY26
APHE30
AALA46
AVAL79
APHE103
AASP104
APHE105
ACYS106

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL B 1001
ChainResidue
BTYR37
BPRO79
BGLY80

site_idAC3
Number of Residues2
Detailsbinding site for residue GOL B 1002
ChainResidue
BLEU52
BLYS99

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGQGTFGEVFkArhrktgqk..........VALK
ChainResidueDetails
AILE25-LYS48

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDMKaaNVLI
ChainResidueDetails
AILE145-ILE157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
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_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18566585","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by EP300/CBP, PCAF/KAT2B and GCN5/KAT2A","evidences":[{"source":"PubMed","id":"17452463","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18250157","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A","evidences":[{"source":"PubMed","id":"18250157","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28426094","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21533037","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CaMK1D","evidences":[{"source":"PubMed","id":"15965233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18483222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18566585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18829461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20535204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20851342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21448926","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21779453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

PDB statisticsPDBj update infoContact PDBjnumon