3MVH
Crystal structure of Akt-1-inhibitor complexes
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 1 |
| Chain | Residue |
| A | GLU314 |
| A | HIS354 |
| A | HOH1034 |
| A | HOH1057 |
| A | HOH1210 |
| B | HOH1045 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE WFE A 999 |
| Chain | Residue |
| A | GLY162 |
| A | VAL164 |
| A | ALA177 |
| A | LEU181 |
| A | MET227 |
| A | GLU228 |
| A | TYR229 |
| A | ALA230 |
| A | GLU234 |
| A | MET281 |
| A | THR291 |
| A | ASP292 |
| A | PHE438 |
| A | HOH1058 |
| A | HOH1149 |
| A | LEU156 |
| A | GLY157 |
| A | LYS158 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 34 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTFGKVIlVkekatgryyamkilkkevIVAK |
| Chain | Residue | Details |
| A | LEU156-LYS189 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDLKleNLML |
| Chain | Residue | Details |
| A | VAL270-LEU282 |
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 | Site: {"description":"Cleavage; by caspase-3","evidences":[{"source":"UniProtKB","id":"P31750","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by TNK2","evidences":[{"source":"PubMed","id":"20333297","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by IKKE, PDPK1 and TBK1","evidences":[{"source":"PubMed","id":"15718470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18456494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20333297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20481595","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21464307","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8978681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9512493","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) threonine","evidences":[{"source":"PubMed","id":"22629392","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22410793","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
