2JFZ
Crystal structure of Helicobacter pylori glutamate racemase in complex with D-Glutamate and an inhibitor
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 | 0042802 | molecular_function | identical protein binding |
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 | 0042802 | molecular_function | identical protein binding |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 003 A1256 |
Chain | Residue |
A | VAL10 |
A | GLN248 |
A | TRP252 |
A | HOH2226 |
A | HOH2227 |
A | GLY11 |
A | PHE13 |
A | ILE149 |
A | SER152 |
A | LEU154 |
A | THR182 |
A | HIS183 |
A | LEU186 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE DGL A1257 |
Chain | Residue |
A | ASP7 |
A | SER8 |
A | VAL37 |
A | PRO38 |
A | TYR39 |
A | GLY40 |
A | CYS70 |
A | ASN71 |
A | THR72 |
A | THR116 |
A | CYS181 |
A | THR182 |
A | HIS183 |
A | HOH2116 |
A | HOH2228 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 003 B1256 |
Chain | Residue |
B | VAL10 |
B | GLY11 |
B | PHE13 |
B | LYS17 |
B | ILE149 |
B | GLU150 |
B | SER152 |
B | LEU154 |
B | HIS183 |
B | LEU186 |
B | GLN248 |
B | TRP252 |
B | HOH2219 |
B | HOH2220 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE DGL B1257 |
Chain | Residue |
B | ASP7 |
B | SER8 |
B | VAL37 |
B | PRO38 |
B | TYR39 |
B | GLY40 |
B | CYS70 |
B | ASN71 |
B | THR72 |
B | THR116 |
B | CYS181 |
B | THR182 |
B | HIS183 |
B | HOH2221 |
B | HOH2222 |
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 | CYS70 | |
A | CYS181 | |
B | CYS70 | |
B | CYS181 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:19097892, ECO:0000269|PubMed:22877632, ECO:0007744|PDB:2JFX, ECO:0007744|PDB:2JFY, ECO:0007744|PDB:2JFZ, ECO:0007744|PDB:2W4I, ECO:0007744|PDB:4B1F |
Chain | Residue | Details |
A | ASP7 | |
A | TYR39 | |
A | ASN71 | |
A | THR182 | |
B | ASP7 | |
B | TYR39 | |
B | ASN71 | |
B | THR182 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1b73 |
Chain | Residue | Details |
A | CYS181 | |
A | SER8 | |
A | ASP7 | |
A | CYS70 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1b73 |
Chain | Residue | Details |
B | CYS181 | |
B | SER8 | |
B | ASP7 | |
B | CYS70 |