1OY0
The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping
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 | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 901 |
| Chain | Residue |
| A | ASP62 |
| A | GLU133 |
| A | HOH914 |
| A | HOH928 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 902 |
| Chain | Residue |
| B | ASP62 |
| B | GLU133 |
| B | HOH911 |
| B | HOH920 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 903 |
| Chain | Residue |
| C | GLU133 |
| C | HOH914 |
| C | HOH922 |
| C | ASP62 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 904 |
| Chain | Residue |
| D | ASP62 |
| D | GLU133 |
| D | HOH917 |
| D | HOH923 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG E 905 |
| Chain | Residue |
| E | ASP62 |
| E | GLU133 |
| E | HOH924 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
