8H4R
The Crystal Structure of CDK3 and CyclinE1 Complex with Dinaciclib from Biortus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000082 | biological_process | G1/S transition of mitotic cell cycle |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000307 | cellular_component | cyclin-dependent protein kinase holoenzyme complex |
A | 0004364 | molecular_function | glutathione transferase activity |
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 | 0005737 | cellular_component | cytoplasm |
A | 0006468 | biological_process | protein phosphorylation |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0006974 | biological_process | DNA damage response |
A | 0007165 | biological_process | signal transduction |
A | 0008283 | biological_process | 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 | 0016301 | molecular_function | kinase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0030332 | molecular_function | cyclin binding |
A | 0045023 | biological_process | G0 to G1 transition |
A | 0045746 | biological_process | negative regulation of Notch signaling pathway |
A | 0051301 | biological_process | cell division |
A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkAknretgql..........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. ViHrDLKpqNLLI |
Chain | Residue | Details |
A | VAL123-ILE135 |
site_id | PS00292 |
Number of Residues | 32 |
Details | CYCLINS Cyclins signature. RaiLldWLmevcevykLhretFylAQdFFDRY |
Chain | Residue | Details |
B | ARG145-TYR176 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |