Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004707 | molecular_function | MAP kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004707 | molecular_function | MAP kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 35F A 1 |
| Chain | Residue |
| A | ALA53 |
| B | LYS30 |
| B | ASN51 |
| B | LEU110 |
| A | GLU109 |
| A | LEU110 |
| A | MET111 |
| A | ASP112 |
| A | ALA113 |
| A | ASN114 |
| A | LEU168 |
| A | HOH454 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 35F B 2 |
| Chain | Residue |
| A | LYS30 |
| A | ASN51 |
| B | GLU109 |
| B | MET111 |
| B | ASP112 |
| B | ALA113 |
| B | HOH555 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpsNIVV |
| Chain | Residue | Details |
| A | ILE147-VAL159 | |
| site_id | PS01351 |
| Number of Residues | 103 |
| Details | MAPK MAP kinase signature. FqnqthakrayRElvllkcvnhkniisllnvftpqktleefqdvylvmelmdanlcqvihmeldhermsyllyqmlcgikhlhsagiih..........RDlKpsnivvksdC |
| Chain | Residue | Details |
| A | PHE61-CYS163 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Motif: {"description":"TXY"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by MAP2K7","evidences":[{"source":"PubMed","id":"11062067","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by MAP2K4","evidences":[{"source":"PubMed","id":"11062067","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | SER155 | |
| A | ASP151 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | SER155 | |
| B | ASP151 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP151 | |
| A | LYS153 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP151 | |
| B | LYS153 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP151 | |
| A | THR188 | |
| A | LYS153 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP151 | |
| B | THR188 | |
| B | LYS153 | |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN156 | |
| A | ASP151 | |
| A | LYS153 | |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN156 | |
| B | ASP151 | |
| B | LYS153 | |
