3DY7
X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 9001 |
| Chain | Residue |
| A | ASN195 |
| A | ASP208 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP A 9000 |
| Chain | Residue |
| A | MET143 |
| A | GLU144 |
| A | MET146 |
| A | SER150 |
| A | GLN153 |
| A | LYS192 |
| A | SER194 |
| A | ASN195 |
| A | LEU197 |
| A | ASP208 |
| A | LEU74 |
| A | GLY75 |
| A | GLY77 |
| A | ASN78 |
| A | GLY80 |
| A | ALA95 |
| A | LYS97 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1CX A 9002 |
| Chain | Residue |
| A | GLY80 |
| A | LYS97 |
| A | ILE141 |
| A | ASP208 |
| A | PHE209 |
| A | SER212 |
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 | 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 | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15543157","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17880056","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18951019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19019675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19706763","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21310613","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19161339","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3EQH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19161339","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3EQF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by BRAF and RAF1","evidences":[{"source":"PubMed","id":"10409742","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20956560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29433126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8131746","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | SER194 | |
| A | ASP190 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS192 | |
| A | ASP190 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS192 | |
| A | THR226 | |
| A | ASP190 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS192 | |
| A | ASN195 | |
| A | ASP190 |
