4RKS
Crystal Structure of Mevalonate-3-Kinase from Thermoplasma acidophilum (Mevalonate Bound)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0008299 | biological_process | isoprenoid biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
A | 0019287 | biological_process | isopentenyl diphosphate biosynthetic process, mevalonate pathway |
B | 0005524 | molecular_function | ATP binding |
B | 0008299 | biological_process | isoprenoid biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
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: BINDING => ECO:0000269|PubMed:25422158, ECO:0007744|PDB:4RKS |
Chain | Residue | Details |
A | LEU19 | |
A | GLU140 | |
A | ARG144 | |
B | LEU19 | |
B | GLU140 | |
B | ARG144 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25422158, ECO:0007744|PDB:4RKZ |
Chain | Residue | Details |
A | TYR96 | |
A | ARG185 | |
B | TYR96 | |
B | ARG185 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25422158, ECO:0007744|PDB:4RKP, ECO:0007744|PDB:4RKZ |
Chain | Residue | Details |
A | SER105 | |
A | SER188 | |
B | SER105 | |
B | SER188 |