3IST
Crystal structure of glutamate racemase from Listeria monocytogenes in complex with succinic acid
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 | 0042802 | molecular_function | identical protein binding |
| 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 | 0042802 | molecular_function | identical protein binding |
| 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 | 13 |
| Details | BINDING SITE FOR RESIDUE SIN A 267 |
| Chain | Residue |
| A | SER10 |
| A | CYS183 |
| A | HOH283 |
| A | HOH358 |
| A | HOH374 |
| A | CYS39 |
| A | PRO40 |
| A | TYR41 |
| A | GLY42 |
| A | THR74 |
| A | THR116 |
| A | THR119 |
| A | VAL147 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SIN B 267 |
| Chain | Residue |
| B | SER10 |
| B | PRO40 |
| B | TYR41 |
| B | GLY42 |
| B | CYS72 |
| B | ASN73 |
| B | THR74 |
| B | HOH270 |
| B | HOH358 |
| B | HOH445 |
| B | HOH446 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 268 |
| Chain | Residue |
| A | HOH273 |
| B | ARG84 |
| B | ILE92 |
| B | GLY93 |
| B | HOH278 |
| B | HOH408 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 268 |
| Chain | Residue |
| A | GLY42 |
| A | THR116 |
| A | LEU117 |
| A | HOH374 |
| A | HOH520 |
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":"UniProtKB","id":"O58403","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P22634","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P22634","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3IST","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1b73 |
| Chain | Residue | Details |
| A | SER10 | |
| A | CYS183 | |
| A | CYS72 | |
| A | ASP9 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1b73 |
| Chain | Residue | Details |
| B | SER10 | |
| B | CYS183 | |
| B | CYS72 | |
| B | ASP9 |
