1O66
Crystal structure of 3-methyl-2-oxobutanoate hydroxymethyltransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003864 | molecular_function | 3-methyl-2-oxobutanoate hydroxymethyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0015940 | biological_process | pantothenate biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003864 | molecular_function | 3-methyl-2-oxobutanoate hydroxymethyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0015940 | biological_process | pantothenate biosynthetic process |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003864 | molecular_function | 3-methyl-2-oxobutanoate hydroxymethyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0015940 | biological_process | pantothenate biosynthetic process |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003864 | molecular_function | 3-methyl-2-oxobutanoate hydroxymethyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0015940 | biological_process | pantothenate biosynthetic process |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003864 | molecular_function | 3-methyl-2-oxobutanoate hydroxymethyltransferase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0015940 | biological_process | pantothenate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 274 |
| Chain | Residue |
| A | ARG61 |
| A | ASP62 |
| B | ARG61 |
| B | ASP62 |
| B | GOL274 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 274 |
| Chain | Residue |
| D | GOL274 |
| C | ARG61 |
| C | ASP62 |
| D | ARG61 |
| D | ASP62 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 274 |
| Chain | Residue |
| A | ARG61 |
| A | ASP62 |
| A | GOL274 |
| B | ARG61 |
| B | ASP62 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 274 |
| Chain | Residue |
| C | ARG61 |
| C | ASP62 |
| C | GOL274 |
| D | ARG61 |
| D | ASP62 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL E 274 |
| Chain | Residue |
| E | ARG61 |
| E | ARG61 |
| E | ASP62 |
| E | ASP62 |
| E | TYR65 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00156","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00156","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
