7UKZ
CDK11 in complex with small molecule inhibitor OTS964
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004674 | molecular_function | protein serine/threonine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
E | 0004672 | molecular_function | protein kinase activity |
E | 0004674 | molecular_function | protein serine/threonine kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006468 | biological_process | protein phosphorylation |
F | 0004672 | molecular_function | protein kinase activity |
F | 0004674 | molecular_function | protein serine/threonine kinase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDLKtsNLLL |
Chain | Residue | Details |
A | ILE202-LEU214 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP206 | |
B | ASP206 | |
C | ASP206 | |
D | ASP206 | |
E | ASP206 | |
F | ASP206 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | ILE88 | |
E | LYS111 | |
F | ILE88 | |
F | LYS111 | |
A | LYS111 | |
B | ILE88 | |
B | LYS111 | |
C | ILE88 | |
C | LYS111 | |
D | ILE88 | |
D | LYS111 | |
E | ILE88 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine; by CDK7 => ECO:0000269|PubMed:16327805 |
Chain | Residue | Details |
A | SER126 | |
B | SER126 | |
C | SER126 | |
D | SER126 | |
E | SER126 | |
F | SER126 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: Phosphothreonine; by CDK7 => ECO:0000269|PubMed:16327805 |
Chain | Residue | Details |
A | THR132 | |
B | THR132 | |
C | THR132 | |
D | THR132 | |
E | THR132 | |
F | THR132 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | SER233 | |
B | SER233 | |
C | SER233 | |
D | SER233 | |
E | SER233 | |
F | SER233 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | TYR238 | |
B | TYR238 | |
C | TYR238 | |
D | TYR238 | |
E | TYR238 | |
F | TYR238 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | TPO239 | |
B | TPO239 | |
C | TPO239 | |
D | TPO239 | |
E | TPO239 | |
F | TPO239 |
site_id | SWS_FT_FI8 |
Number of Residues | 12 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS285 | |
F | LYS285 | |
B | LYS285 | |
C | LYS285 | |
D | LYS285 | |
E | LYS285 |