4AW2
Crystal structure of CDC42 binding protein kinase alpha (MRCK alpha)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 22E A 500 |
| Chain | Residue |
| A | ASP33 |
| A | LYS339 |
| A | HOH2099 |
| A | HOH2210 |
| A | ILE36 |
| A | LYS68 |
| A | GLN69 |
| A | ARG71 |
| A | HIS73 |
| A | GLN145 |
| A | ASP146 |
| A | ASP147 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1418 |
| Chain | Residue |
| A | TYR56 |
| A | TRP59 |
| A | ARG123 |
| A | LEU397 |
| A | PRO398 |
| A | HOH2202 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1419 |
| Chain | Residue |
| A | LYS106 |
| A | LEU108 |
| A | ALA120 |
| A | CYS121 |
| A | GLU125 |
| A | GLY221 |
| A | HOH2063 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1420 |
| Chain | Residue |
| A | ALA104 |
| A | TYR156 |
| A | TYR157 |
| A | HOH2105 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1421 |
| Chain | Residue |
| A | GLU29 |
| A | ARG71 |
| A | CYS408 |
| A | LEU410 |
| A | HOH2206 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVAvVklknadkv..........FAMK |
| Chain | Residue | Details |
| A | ILE83-LYS106 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YvHrDIKpdNILM |
| Chain | Residue | Details |
| A | TYR197-MET209 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 266 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9418861","evidenceCode":"ECO:0000269"}]} |
| 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":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9418861","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q5VT25","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q5VT25","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
