5F9E
Structure of Protein Kinase C theta with compound 10: 2,2-dimethyl-7-(2-oxidanylidene-3~{H}-imidazo[4,5-b]pyridin-1-yl)-1-(phenylmethyl)-3~{H}-quinazolin-4-one
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 | 0004697 | molecular_function | diacylglycerol-dependent 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 | 0004697 | molecular_function | diacylglycerol-dependent serine/threonine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue 5VS A 1001 |
Chain | Residue |
A | LEU386 |
A | LEU461 |
A | ASN509 |
A | LEU511 |
A | ASP522 |
A | PHE664 |
A | GLY387 |
A | PHE391 |
A | VAL394 |
A | ALA407 |
A | LYS409 |
A | THR442 |
A | MET458 |
A | GLU459 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue 5VS B 1001 |
Chain | Residue |
B | LEU386 |
B | PHE391 |
B | ALA407 |
B | LYS409 |
B | THR442 |
B | MET458 |
B | GLU459 |
B | LEU461 |
B | ASN509 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGSFGKVFlAefkktnqf..........FAIK |
Chain | Residue | Details |
A | LEU386-LYS409 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvYrDLKldNILL |
Chain | Residue | Details |
A | ILE500-LEU512 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP504 | |
B | ASP504 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU386 | |
B | LEU386 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS409 | |
B | LYS409 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000305|PubMed:11772397, ECO:0000305|PubMed:15364937, ECO:0000305|PubMed:16252004 |
Chain | Residue | Details |
A | GLU538 | |
B | GLU538 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:11772397, ECO:0000269|PubMed:16252004, ECO:0000269|Ref.38, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SEP676 | |
B | SEP676 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER685 | |
B | SER685 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:11772397, ECO:0000269|PubMed:15364937, ECO:0000269|PubMed:16252004, ECO:0000269|Ref.38, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SEP695 | |
B | SEP695 |