6GZH
Crystal Structure of Human CDK9/cyclinT1 with A86
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0000079 | biological_process | regulation of cyclin-dependent protein serine/threonine kinase activity |
B | 0000307 | cellular_component | cyclin-dependent protein kinase holoenzyme complex |
B | 0000976 | molecular_function | transcription cis-regulatory region binding |
B | 0003677 | molecular_function | DNA binding |
B | 0003682 | molecular_function | chromatin binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005730 | cellular_component | nucleolus |
B | 0005829 | cellular_component | cytosol |
B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
B | 0006366 | biological_process | transcription by RNA polymerase II |
B | 0008024 | cellular_component | cyclin/CDK positive transcription elongation factor complex |
B | 0009410 | biological_process | response to xenobiotic stimulus |
B | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
B | 0017069 | molecular_function | snRNA binding |
B | 0019901 | molecular_function | protein kinase binding |
B | 0032786 | biological_process | positive regulation of DNA-templated transcription, elongation |
B | 0032968 | biological_process | positive regulation of transcription elongation by RNA polymerase II |
B | 0043923 | biological_process | positive regulation by host of viral transcription |
B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
B | 0051301 | biological_process | cell division |
B | 0061575 | molecular_function | cyclin-dependent protein serine/threonine kinase activator activity |
B | 0070063 | molecular_function | RNA polymerase binding |
B | 0070691 | cellular_component | P-TEFb complex |
B | 0097322 | molecular_function | 7SK snRNA binding |
B | 0140297 | molecular_function | DNA-binding transcription factor binding |
B | 0140693 | molecular_function | molecular condensate scaffold activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue LCI A 2001 |
Chain | Residue |
A | ILE25 |
A | GLU107 |
A | ASP109 |
A | LEU156 |
A | HOH2107 |
A | HOH2122 |
A | GLY26 |
A | PHE30 |
A | ALA46 |
A | VAL79 |
A | PHE103 |
A | ASP104 |
A | PHE105 |
A | CYS106 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue GOL B 1001 |
Chain | Residue |
B | TYR37 |
B | PRO79 |
B | GLY80 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue GOL B 1002 |
Chain | Residue |
B | LEU52 |
B | LYS99 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGQGTFGEVFkArhrktgqk..........VALK |
Chain | Residue | Details |
A | ILE25-LYS48 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDMKaaNVLI |
Chain | Residue | Details |
A | ILE145-ILE157 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Essential for interacting with HIV-1 Tat |
Chain | Residue | Details |
B | CYS261 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
B | SER117 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER340 | |
A | ASP104 | |
A | ASP167 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER388 | |
B | SER564 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
B | LYS390 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: ADP-ribosylserine => ECO:0000269|PubMed:35393539 |
Chain | Residue | Details |
B | SER416 | |
B | SER474 | |
B | SER475 | |
B | SER531 | |
B | SER549 | |
B | SER552 | |
B | SER563 | |
B | SER637 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N6-(ADP-ribosyl)lysine => ECO:0000269|PubMed:35393539 |
Chain | Residue | Details |
B | LYS485 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | MOD_RES: ADP-ribosylhistidine => ECO:0000269|PubMed:35393539 |
Chain | Residue | Details |
B | HIS487 | |
B | HIS530 | |
B | HIS556 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976 |
Chain | Residue | Details |
B | SER495 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
B | SER499 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER577 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS342 | |
B | LYS415 | |
B | LYS481 |