7JUV
Crystal Structure of KSR2:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor APS-9-95-1
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0000165 | biological_process | MAPK cascade |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0004708 | molecular_function | MAP kinase kinase activity |
C | 0004713 | molecular_function | protein tyrosine kinase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005769 | cellular_component | early endosome |
C | 0005770 | cellular_component | late endosome |
C | 0005813 | cellular_component | centrosome |
C | 0005816 | cellular_component | spindle pole body |
C | 0005856 | cellular_component | cytoskeleton |
C | 0005925 | cellular_component | focal adhesion |
C | 0006468 | biological_process | protein phosphorylation |
C | 0016020 | cellular_component | membrane |
C | 0016310 | biological_process | phosphorylation |
C | 0032872 | biological_process | regulation of stress-activated MAPK cascade |
C | 0090170 | biological_process | regulation of Golgi inheritance |
C | 0106310 | molecular_function | protein serine kinase activity |
C | 2000641 | biological_process | regulation of early endosome to late endosome transport |
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 |
C | LEU74-LYS97 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHkDLKskNVFY |
Chain | Residue | Details |
B | ILE782-TYR794 | |
C | 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 |
C | ASP190 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:21441910 |
Chain | Residue | Details |
C | LEU74 | |
C | LYS97 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by RAF => ECO:0000269|PubMed:8157000 |
Chain | Residue | Details |
C | SER218 | |
C | SER222 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q02750 |
Chain | Residue | Details |
C | THR286 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by MAPK1 => ECO:0000250|UniProtKB:Q01986 |
Chain | Residue | Details |
C | THR292 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PAK => ECO:0000250|UniProtKB:Q02750 |
Chain | Residue | Details |
C | SER298 |