9AYA
Crystal structure of CRAF/MEK complex with NST-628 and active 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. IGSGSFGTVYkGkwhgd.............VAVK |
Chain | Residue | Details |
A | ILE355-LYS375 | |
B | LEU74-LYS97 |
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 |
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 | |
D | ASP208 | |
B | MET143 | |
B | SER150 | |
B | LYS192 | |
B | ASP208 | |
D | LEU74 | |
D | MET143 | |
D | SER150 | |
D | LYS192 |
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 | 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 | |
C | ASP340 | |
C | ASP341 |
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 |
B | ALA222 | |
D | ALA222 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:11447113 |
Chain | Residue | Details |
A | THR491 | |
C | THR491 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:11447113 |
Chain | Residue | Details |
A | SER494 | |
C | SER494 |
site_id | SWS_FT_FI9 |
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_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:21917714 |
Chain | Residue | Details |
A | ARG563 | |
C | ARG563 |