21OA
Crystal structure of human MEK2 in complex with Refametinib
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVTkVqhrpsgli..........MARK |
| Chain | Residue | Details |
| A | LEU78-LYS101 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKpsNILV |
| Chain | Residue | Details |
| A | ILE190-VAL202 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 54 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine; by RAF; alternate","evidences":[{"source":"PubMed","id":"10409742","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17116858","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; alternate","evidences":[{"source":"PubMed","id":"17116858","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 282 |
| Chain | Residue | Details |
| A | ASP194 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP221 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 282 |
| Chain | Residue | Details |
| B | ASP194 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP221 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 282 |
| Chain | Residue | Details |
| C | ASP194 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ASP221 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 282 |
| Chain | Residue | Details |
| D | ASP194 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ASP221 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| site_id | MCSA5 |
| Number of Residues | 2 |
| Details | M-CSA 282 |
| Chain | Residue | Details |
| E | ASP194 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | ASP221 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| site_id | MCSA6 |
| Number of Residues | 2 |
| Details | M-CSA 282 |
| Chain | Residue | Details |
| F | ASP194 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | ASP221 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
