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 |