4UAK
MRCK beta in complex with ADP
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue ADP A 501 |
| Chain | Residue |
| A | ILE82 |
| A | ASN205 |
| A | LEU207 |
| A | ASP218 |
| A | PHE370 |
| A | MG502 |
| A | MG503 |
| A | HOH777 |
| A | HOH778 |
| A | HOH779 |
| A | HOH792 |
| A | ALA103 |
| A | LYS105 |
| A | MET153 |
| A | ASP154 |
| A | TYR155 |
| A | TYR156 |
| A | ASP160 |
| A | ASP204 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | ASP218 |
| A | ADP501 |
| A | HOH737 |
| A | HOH777 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 503 |
| Chain | Residue |
| A | ASN205 |
| A | ASP218 |
| A | ADP501 |
| A | HOH778 |
| A | HOH779 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | PHE391 |
| A | PHE391 |
| A | LYS416 |
| A | LYS416 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | VAL157 |
| A | VAL210 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | LYS105 |
| A | LEU107 |
| A | ALA119 |
| A | CYS120 |
| A | GLU124 |
| A | GLY220 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVAvVkmknteri..........YAMK |
| Chain | Residue | Details |
| A | ILE82-LYS105 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YvHrDIKpdNVLL |
| Chain | Residue | Details |
| A | TYR196-LEU208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 266 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"UniProtKB","id":"Q5VT25","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P54265","evidenceCode":"ECO:0000250"},{"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 | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P54265","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q5VT25","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
