4RKS
Crystal Structure of Mevalonate-3-Kinase from Thermoplasma acidophilum (Mevalonate Bound)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0019287 | biological_process | isopentenyl diphosphate biosynthetic process, mevalonate pathway |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0019287 | biological_process | isopentenyl diphosphate biosynthetic process, mevalonate pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MEV A 401 |
| Chain | Residue |
| A | GLY15 |
| A | LEU18 |
| A | LEU19 |
| A | GLU140 |
| A | SER141 |
| A | ARG144 |
| A | HIS192 |
| A | TYR238 |
| A | GLY276 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | TYR183 |
| A | GLN184 |
| A | ARG251 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | ARG251 |
| A | GLU252 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MEV B 401 |
| Chain | Residue |
| B | GLY15 |
| B | LEU18 |
| B | LEU19 |
| B | GLU140 |
| B | SER141 |
| B | ARG144 |
| B | TYR238 |
| B | HOH569 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 402 |
| Chain | Residue |
| B | SER105 |
| B | GLY106 |
| B | SER107 |
| B | SER108 |
| B | ARG185 |
| B | HOH571 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 403 |
| Chain | Residue |
| B | ARG251 |
| B | GLU252 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 404 |
| Chain | Residue |
| B | GLN184 |
| B | LYS206 |
| B | ARG251 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 405 |
| Chain | Residue |
| A | ARG316 |
| A | HOH553 |
| B | TYR53 |
| B | SER97 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25422158","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RKS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25422158","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RKZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25422158","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RKP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RKZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
