5HZE
Mek1 adopts DFG-out conformation when bound to an analog of E6201.
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue E62 A 401 |
| Chain | Residue |
| A | LEU74 |
| A | ASN195 |
| A | LEU197 |
| A | CYS207 |
| A | PHE209 |
| A | ALA95 |
| A | LYS97 |
| A | MET143 |
| A | GLU144 |
| A | HIS145 |
| A | MET146 |
| A | GLY149 |
| A | SER194 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ASP65 |
| A | ASP66 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASP65 |
| A | ASP65 |
| A | ASP66 |
| A | ASP66 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK |
| Chain | Residue | Details |
| A | LEU74-LYS97 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKpsNILV |
| Chain | Residue | Details |
| A | ILE186-VAL198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP190 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15543157, ECO:0000269|PubMed:17880056, ECO:0000269|PubMed:18951019, ECO:0000269|PubMed:19019675, ECO:0000269|PubMed:19706763, ECO:0000269|PubMed:21310613 |
| Chain | Residue | Details |
| A | LEU74 | |
| A | MET143 | |
| A | SER150 | |
| A | LYS192 | |
| A | ASP208 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQH |
| Chain | Residue | Details |
| A | LYS97 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF |
| Chain | Residue | Details |
| A | GLU144 | |
| A | SER194 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| 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 | SER218 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746 |
| Chain | Residue | Details |
| A | SER222 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976 |
| Chain | Residue | Details |
| A | THR286 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by MAPK1 => ECO:0000250|UniProtKB:Q01986 |
| Chain | Residue | Details |
| A | THR292 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PAK => ECO:0000269|PubMed:16129686 |
| Chain | Residue | Details |
| A | ASN298 |
