9AXM
Crystal structure of ARAF/MEK1 complex with NST-628 and a RAF dimer
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 21 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGTGSFGTVFrGrwhgd.............VAVK |
| Chain | Residue | Details |
| B | ILE316-LYS336 | |
| A | LEU74-LYS97 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL |
| Chain | Residue | Details |
| B | ILE425-LEU437 | |
| A | ILE186-VAL198 |
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 |
| B | ASP429 | |
| D | ASP429 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| B | ILE316 | |
| C | ASP208 | |
| B | LYS336 | |
| D | ILE316 | |
| D | LYS336 | |
| A | ASP208 | |
| C | LEU74 | |
| C | MET143 | |
| C | SER150 | |
| C | LYS192 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| B | THR318 | |
| D | THR318 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF |
| Chain | Residue | Details |
| A | GLU144 | |
| A | SER194 | |
| C | GLU144 | |
| C | SER194 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746 |
| Chain | Residue | Details |
| A | ALA218 | |
| C | ALA218 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746 |
| Chain | Residue | Details |
| A | ALA222 | |
| C | ALA222 |
