9AXC
Activated CRAF/MEK heterotetramer from focused refinement of CRAF/MEK/14-3-3 complex
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 21 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK |
| Chain | Residue | Details |
| B | LEU74-LYS97 | |
| A | ILE355-LYS375 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDMKsnNIFL |
| Chain | Residue | Details |
| A | ILE464-LEU476 | |
| B | 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 | ASP190 | |
| D | ASP190 | |
| A | ASN139 | |
| A | GLN152 | |
| C | TYR92 | |
| C | TRP126 | |
| C | ASN139 | |
| C | GLN152 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| 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 |
| B | LEU74 | |
| B | MET143 | |
| B | SER150 | |
| B | LYS192 | |
| B | ASP208 | |
| D | LEU74 | |
| D | MET143 | |
| D | SER150 | |
| D | LYS192 | |
| D | ASP208 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQH |
| Chain | Residue | Details |
| B | LYS97 | |
| D | LYS97 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF |
| Chain | Residue | Details |
| B | GLU144 | |
| B | SER194 | |
| D | GLU144 | |
| D | SER194 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by anthrax lethal factor |
| Chain | Residue | Details |
| B | PRO8 | |
| D | PRO8 |
| site_id | SWS_FT_FI6 |
| 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 |
| B | ALA218 | |
| D | ALA218 |
| site_id | SWS_FT_FI7 |
| 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 |
| B | ALA222 | |
| D | ALA222 | |
| C | ASP340 | |
| C | ASP341 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976 |
| Chain | Residue | Details |
| B | THR286 | |
| D | THR286 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by MAPK1 => ECO:0000250|UniProtKB:Q01986 |
| Chain | Residue | Details |
| B | THR292 | |
| D | THR292 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PAK => ECO:0000269|PubMed:16129686 |
| Chain | Residue | Details |
| B | SER298 | |
| D | SER298 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8349614 |
| Chain | Residue | Details |
| A | SER499 | |
| C | SER499 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:21917714 |
| Chain | Residue | Details |
| A | ARG563 | |
| C | ARG563 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:8349614 |
| Chain | Residue | Details |
| A | SER621 | |
| C | SER621 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by MAPK1 => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER642 | |
| C | SER642 |
