5YT3
Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D mutant
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 PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue ANP A 401 |
| Chain | Residue |
| A | ALA76 |
| A | GLN153 |
| A | ASP190 |
| A | LYS192 |
| A | SER194 |
| A | ASN195 |
| A | LEU197 |
| A | ASP208 |
| A | MG402 |
| A | GLY80 |
| A | VAL82 |
| A | ALA95 |
| A | LYS97 |
| A | MET143 |
| A | GLU144 |
| A | MET146 |
| A | SER150 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ASN195 |
| A | ASP208 |
| A | ANP401 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue ANP B 401 |
| Chain | Residue |
| B | LEU74 |
| B | GLY75 |
| B | ALA76 |
| B | GLY77 |
| B | ASN78 |
| B | GLY79 |
| B | VAL82 |
| B | ALA95 |
| B | LYS97 |
| B | GLU144 |
| B | MET146 |
| B | SER150 |
| B | GLN153 |
| B | LYS192 |
| B | SER194 |
| B | ASN195 |
| B | LEU197 |
| B | ASP208 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue ANP C 401 |
| Chain | Residue |
| C | LEU74 |
| C | GLY77 |
| C | GLY80 |
| C | VAL82 |
| C | ALA95 |
| C | LYS97 |
| C | GLU144 |
| C | MET146 |
| C | SER150 |
| C | GLN153 |
| C | ASP190 |
| C | LYS192 |
| C | SER194 |
| C | ASN195 |
| C | LEU197 |
| C | ASP208 |
| C | MG402 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 402 |
| Chain | Residue |
| C | SER194 |
| C | ASN195 |
| C | ASP208 |
| C | ANP401 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | binding site for residue ANP D 401 |
| Chain | Residue |
| D | LEU74 |
| D | GLY75 |
| D | GLY77 |
| D | ASN78 |
| D | VAL82 |
| D | ALA95 |
| D | LYS97 |
| D | MET143 |
| D | GLU144 |
| D | MET146 |
| D | SER150 |
| D | GLN153 |
| D | LYS192 |
| D | SER194 |
| D | ASN195 |
| D | LEU197 |
| D | CYS207 |
| D | HOH502 |
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 | 4 |
| 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 | 72 |
| 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 | 13 |
| 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 | 12 |
| 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 | 2 |
| 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 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by BRAF and RAF1","evidences":[{"source":"PubMed","id":"20956560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29433126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8131746","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






