2C6O
Crystal structure of the human CDK2 complexed with the triazolopyrimidine inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000082 | biological_process | G1/S transition of mitotic cell cycle |
| A | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
| A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000307 | cellular_component | cyclin-dependent protein kinase holoenzyme complex |
| A | 0000781 | cellular_component | chromosome, telomeric region |
| A | 0000793 | cellular_component | condensed chromosome |
| A | 0000805 | cellular_component | X chromosome |
| A | 0000806 | cellular_component | Y chromosome |
| A | 0001673 | cellular_component | male germ cell nucleus |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004693 | molecular_function | cyclin-dependent protein serine/threonine kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005635 | cellular_component | nuclear envelope |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005667 | cellular_component | transcription regulator complex |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005768 | cellular_component | endosome |
| A | 0005813 | cellular_component | centrosome |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0006260 | biological_process | DNA replication |
| A | 0006281 | biological_process | DNA repair |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0006813 | biological_process | potassium ion transport |
| A | 0007099 | biological_process | centriole replication |
| A | 0007165 | biological_process | signal transduction |
| A | 0007265 | biological_process | Ras protein signal transduction |
| A | 0007346 | biological_process | regulation of mitotic cell cycle |
| A | 0008284 | biological_process | positive regulation of cell population proliferation |
| A | 0010389 | biological_process | regulation of G2/M transition of mitotic cell cycle |
| A | 0010468 | biological_process | regulation of gene expression |
| A | 0015030 | cellular_component | Cajal body |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0018105 | biological_process | peptidyl-serine phosphorylation |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0030332 | molecular_function | cyclin binding |
| A | 0031453 | biological_process | positive regulation of heterochromatin formation |
| A | 0031571 | biological_process | mitotic G1 DNA damage checkpoint signaling |
| A | 0032298 | biological_process | positive regulation of DNA-templated DNA replication initiation |
| A | 0035173 | molecular_function | histone kinase activity |
| A | 0043247 | biological_process | telomere maintenance in response to DNA damage |
| A | 0043687 | biological_process | post-translational protein modification |
| A | 0045740 | biological_process | positive regulation of DNA replication |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051298 | biological_process | centrosome duplication |
| A | 0051301 | biological_process | cell division |
| A | 0051321 | biological_process | meiotic cell cycle |
| A | 0071732 | biological_process | cellular response to nitric oxide |
| A | 0090398 | biological_process | cellular senescence |
| A | 0097123 | cellular_component | cyclin A1-CDK2 complex |
| A | 0097124 | cellular_component | cyclin A2-CDK2 complex |
| A | 0097134 | cellular_component | cyclin E1-CDK2 complex |
| A | 0097135 | cellular_component | cyclin E2-CDK2 complex |
| A | 0097472 | molecular_function | cyclin-dependent protein kinase activity |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 1905784 | biological_process | regulation of anaphase-promoting complex-dependent catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 4SP A1297 |
| Chain | Residue |
| A | ILE10 |
| A | HIS84 |
| A | GLN85 |
| A | ASP86 |
| A | LYS89 |
| A | GLN131 |
| A | LEU134 |
| A | HOH2011 |
| A | HOH2060 |
| A | GLY13 |
| A | VAL18 |
| A | ALA31 |
| A | LYS33 |
| A | PHE80 |
| A | GLU81 |
| A | PHE82 |
| A | LEU83 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK |
| Chain | Residue | Details |
| A | ILE10-LYS33 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI |
| Chain | Residue | Details |
| A | VAL123-ILE135 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | ASP127 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 |
| Chain | Residue | Details |
| A | ILE10 | |
| A | LYS33 | |
| A | GLU81 | |
| A | ASP86 | |
| A | LYS129 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21565702 |
| Chain | Residue | Details |
| A | ASN132 | |
| A | ASP145 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | SITE: CDK7 binding => ECO:0000269|PubMed:17373709 |
| Chain | Residue | Details |
| A | LYS9 | |
| A | LYS88 | |
| A | LEU166 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | MET1 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS6 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507 |
| Chain | Residue | Details |
| A | THR14 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by WEE1 => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507, ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | TYR15 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | TYR19 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by CAK and CCRK => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17570665, ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:21565702, ECO:0000305|PubMed:28666995 |
| Chain | Residue | Details |
| A | THR160 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | GLN131 | |
| A | ASP127 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP127 | |
| A | LYS129 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP127 | |
| A | LYS129 | |
| A | THR165 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP127 | |
| A | LYS129 | |
| A | ASN132 |
