3E8D
Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE G98 A 1 |
| Chain | Residue |
| A | LYS160 |
| A | PHE227 |
| A | MET229 |
| A | GLU230 |
| A | TYR231 |
| A | ALA232 |
| A | ASN280 |
| A | MET282 |
| A | THR292 |
| A | ASP293 |
| A | PHE294 |
| A | GLY161 |
| A | PHE439 |
| C | SER9 |
| A | GLY164 |
| A | LYS165 |
| A | VAL166 |
| A | ALA179 |
| A | LYS181 |
| A | GLU200 |
| A | LEU204 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE G98 B 1 |
| Chain | Residue |
| B | GLY161 |
| B | GLY164 |
| B | VAL166 |
| B | ALA179 |
| B | LYS181 |
| B | GLU200 |
| B | LEU204 |
| B | PHE227 |
| B | MET229 |
| B | GLU230 |
| B | TYR231 |
| B | ALA232 |
| B | ASN280 |
| B | MET282 |
| B | THR292 |
| B | ASP293 |
| B | PHE294 |
| B | PHE439 |
| D | SER9 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 34 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTFGKVIlVrekatgryyamkilrkevIIAK |
| Chain | Residue | Details |
| A | LEU158-LYS191 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDIKleNLML |
| Chain | Residue | Details |
| A | VAL271-LEU283 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| 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 | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12434148","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"12434148","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15890450","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20059950","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9512493","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) threonine","evidences":[{"source":"UniProtKB","id":"P31749","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK3","evidences":[{"source":"PubMed","id":"12054501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16484495","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20937854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24391509","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25169422","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35606353","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8250835","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | GLU279 | |
| A | ASP275 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | GLU279 | |
| B | ASP275 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS277 | |
| A | ASP275 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS277 | |
| B | ASP275 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR313 | |
| A | LYS277 | |
| A | ASP275 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR313 | |
| B | LYS277 | |
| B | ASP275 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN280 | |
| A | LYS277 | |
| A | ASP275 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN280 | |
| B | LYS277 | |
| B | ASP275 |
