2JFQ
Crystal structure of Staphylococcus aureus glutamate racemase in complex with D- Glutamate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| 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 | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0071555 | biological_process | cell wall organization |
| B | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| 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 | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
| B | 0042802 | molecular_function | identical protein binding |
| 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 1267 |
| Chain | Residue |
| A | ASP9 |
| A | CYS184 |
| A | THR185 |
| A | HIS186 |
| A | HOH2002 |
| A | HOH2039 |
| A | SER10 |
| A | PRO40 |
| A | TYR41 |
| A | GLY42 |
| A | CYS72 |
| A | ASN73 |
| A | THR74 |
| A | THR116 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGL B 1267 |
| Chain | Residue |
| B | ASP9 |
| B | SER10 |
| B | PRO40 |
| B | TYR41 |
| B | GLY42 |
| B | CYS72 |
| B | ASN73 |
| B | THR74 |
| B | THR116 |
| B | CYS184 |
| B | THR185 |
| B | HIS186 |
| B | HOH2003 |
| B | HOH2061 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-Rule:MF_00258 |
| Chain | Residue | Details |
| A | CYS72 | |
| A | CYS184 | |
| B | CYS72 | |
| B | CYS184 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFQ |
| Chain | Residue | Details |
| A | ASP9 | |
| A | TYR41 | |
| A | ASN73 | |
| A | THR185 | |
| B | ASP9 | |
| B | TYR41 | |
| B | ASN73 | |
| B | THR185 |
