5IJW
Glutamate Racemase (MurI) from Mycobacterium smegmatis with bound D-glutamate, 1.8 Angstrom resolution, X-ray diffraction
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008881 | molecular_function | glutamate racemase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| A | 0047661 | molecular_function | amino-acid racemase activity |
| A | 0071555 | biological_process | cell wall organization |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008881 | molecular_function | glutamate racemase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| B | 0047661 | molecular_function | amino-acid racemase activity |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue DGL A 301 |
| Chain | Residue |
| A | ASP12 |
| A | CYS186 |
| A | THR187 |
| A | HIS188 |
| A | HOH448 |
| A | HOH454 |
| A | SER13 |
| A | PRO43 |
| A | TYR44 |
| A | GLY45 |
| A | CYS75 |
| A | ASN76 |
| A | THR77 |
| A | THR120 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue IOD A 302 |
| Chain | Residue |
| A | GLY45 |
| A | GLN121 |
| A | PRO147 |
| A | HOH491 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 303 |
| Chain | Residue |
| A | PRO261 |
| B | ARG240 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 304 |
| Chain | Residue |
| A | ALA250 |
| A | HOH657 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue DGL B 301 |
| Chain | Residue |
| B | ASP12 |
| B | SER13 |
| B | PRO43 |
| B | TYR44 |
| B | GLY45 |
| B | CYS75 |
| B | ASN76 |
| B | THR77 |
| B | THR120 |
| B | CYS186 |
| B | THR187 |
| B | HIS188 |
| B | HOH443 |
| B | HOH452 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
