6YLC
Biochemical, Cellular and Structural Characterization of Novel ERK3 Inhibitors
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 |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004707 | molecular_function | MAP kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004707 | molecular_function | MAP 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 | 13 |
| Details | binding site for residue OXW A 401 |
| Chain | Residue |
| A | LEU26 |
| A | THR113 |
| A | ASP114 |
| A | PHE159 |
| C | ASP164 |
| A | GLY27 |
| A | CYS28 |
| A | GLY29 |
| A | ALA47 |
| A | GLN108 |
| A | GLU109 |
| A | MET111 |
| A | GLU112 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue OXW B 401 |
| Chain | Residue |
| B | LEU26 |
| B | GLY27 |
| B | CYS28 |
| B | VAL34 |
| B | ALA47 |
| B | GLN108 |
| B | GLU109 |
| B | TYR110 |
| B | MET111 |
| B | GLU112 |
| B | PHE159 |
| B | ASP171 |
| B | HOH512 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue OXW C 401 |
| Chain | Residue |
| C | LEU26 |
| C | ASN31 |
| C | ALA47 |
| C | LYS49 |
| C | GLN108 |
| C | GLU109 |
| C | MET111 |
| C | GLU112 |
| C | ASP114 |
| C | PHE159 |
| C | ASP171 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue OXW D 401 |
| Chain | Residue |
| D | ASN31 |
| D | VAL34 |
| D | LYS49 |
| D | GLU109 |
| D | TYR110 |
| D | MET111 |
| D | GLU112 |
| D | PHE159 |
| D | PHE172 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGCGGNGLVFsAvdndcdkrv.........AIKK |
| Chain | Residue | Details |
| A | LEU26-LYS50 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpaNLFI |
| Chain | Residue | Details |
| A | VAL148-ILE160 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Motif: {"description":"SEG motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by PAK1, PAK2 and PAK3","evidences":[{"source":"PubMed","id":"21177870","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
