3ISV
Crystal structure of glutamate racemase from Listeria monocytogenes in complex with acetate ion
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 | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
| 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 | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 267 |
| Chain | Residue |
| A | SER10 |
| A | PRO40 |
| A | TYR41 |
| A | GLY42 |
| A | VAL147 |
| A | CYS183 |
| A | HOH333 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 268 |
| Chain | Residue |
| A | HOH368 |
| A | HOH381 |
| B | PHE59 |
| B | ILE262 |
| B | LYS263 |
| B | HOH329 |
| A | ARG135 |
| A | HOH341 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 269 |
| Chain | Residue |
| A | LYS2 |
| A | HOH380 |
| A | HOH382 |
| A | HOH383 |
| A | HOH409 |
| A | HOH464 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 270 |
| Chain | Residue |
| A | GLU137 |
| A | HOH341 |
| A | HOH381 |
| A | HOH461 |
| B | GLU260 |
| B | HIS261 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 271 |
| Chain | Residue |
| A | THR74 |
| A | THR116 |
| A | THR119 |
| A | HOH280 |
| A | HOH318 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 272 |
| Chain | Residue |
| A | THR116 |
| A | LEU117 |
| A | HOH333 |
| B | HOH308 |
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 | CYS183 | |
| B | CYS72 | |
| B | CYS183 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-Rule:MF_00258 |
| Chain | Residue | Details |
| A | ASP9 | |
| A | ASN73 | |
| A | THR184 | |
| B | ASP9 | |
| B | ASN73 | |
| B | THR184 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-Rule:MF_00258, ECO:0007744|PDB:3IST |
| Chain | Residue | Details |
| A | TYR41 | |
| B | TYR41 |
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 |
