3UHF
Crystal Structure of Glutamate Racemase from Campylobacter jejuni subsp. jejuni
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 | 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 | 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 260 |
| Chain | Residue |
| A | ASP7 |
| A | CYS180 |
| A | THR181 |
| A | HIS182 |
| A | HOH254 |
| A | HOH318 |
| A | SER8 |
| A | PRO38 |
| A | TYR39 |
| A | GLY40 |
| A | CYS70 |
| A | ASN71 |
| A | THR72 |
| A | THR116 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 261 |
| Chain | Residue |
| A | SER74 |
| A | ALA75 |
| A | TYR76 |
| A | ALA77 |
| A | LEU78 |
| A | ASP79 |
| A | GLU124 |
| A | HOH330 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 262 |
| Chain | Residue |
| A | GLY40 |
| A | VAL41 |
| A | LYS42 |
| A | LYS117 |
| A | ALA118 |
| A | LYS121 |
| B | HOH357 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 263 |
| Chain | Residue |
| A | ARG82 |
| A | GLY91 |
| A | HOH253 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 264 |
| Chain | Residue |
| A | ARG128 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGL B 260 |
| Chain | Residue |
| B | ASP7 |
| B | SER8 |
| B | PRO38 |
| B | TYR39 |
| B | GLY40 |
| B | CYS70 |
| B | ASN71 |
| B | THR72 |
| B | THR116 |
| B | CYS180 |
| B | THR181 |
| B | HIS182 |
| B | HOH251 |
| B | HOH306 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 261 |
| Chain | Residue |
| B | SER74 |
| B | ALA75 |
| B | TYR76 |
| B | ALA77 |
| B | LEU78 |
| B | ASP79 |
| B | HOH335 |
| B | HOH366 |
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 | CYS180 | |
| B | CYS70 | |
| B | CYS180 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|Ref.2, ECO:0007744|PDB:3UHF, ECO:0007744|PDB:3UHO |
| Chain | Residue | Details |
| A | ASP7 | |
| A | TYR39 | |
| A | ASN71 | |
| A | THR181 | |
| B | ASP7 | |
| B | TYR39 | |
| B | ASN71 | |
| B | THR181 |
