3OJC
Crystal structure of a putative Asp/Glu Racemase from Yersinia pestis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006807 | biological_process | obsolete nitrogen compound metabolic 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 | 0046872 | molecular_function | metal ion binding |
| A | 0047661 | molecular_function | amino-acid racemase activity |
| B | 0006807 | biological_process | obsolete nitrogen compound metabolic 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 | 0046872 | molecular_function | metal ion binding |
| B | 0047661 | molecular_function | amino-acid racemase activity |
| C | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| C | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047661 | molecular_function | amino-acid racemase activity |
| D | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| D | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047661 | molecular_function | amino-acid racemase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 232 |
| Chain | Residue |
| A | GLY125 |
| A | THR126 |
| A | THR129 |
| A | GLY197 |
| A | CYS198 |
| A | HOH291 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 233 |
| Chain | Residue |
| B | GLN115 |
| A | PRO213 |
| A | VAL214 |
| A | HOH387 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 232 |
| Chain | Residue |
| B | GLY125 |
| B | THR126 |
| B | THR129 |
| B | GLY197 |
| B | HOH306 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 234 |
| Chain | Residue |
| A | ASP119 |
| A | GLY144 |
| A | HOH253 |
| A | HOH479 |
| A | HOH620 |
| A | HOH646 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HEZ A 235 |
| Chain | Residue |
| A | GLN25 |
| A | HIS26 |
| A | HOH366 |
| A | HOH641 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HEZ A 236 |
| Chain | Residue |
| A | LYS73 |
| A | HIS74 |
| A | HEZ237 |
| A | HOH249 |
| A | HOH552 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HEZ B 233 |
| Chain | Residue |
| B | GLU187 |
| B | SER211 |
| B | HEZ236 |
| B | HOH625 |
| D | GLN59 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE HEZ D 232 |
| Chain | Residue |
| D | GLN25 |
| D | HIS26 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE HEZ C 232 |
| Chain | Residue |
| A | SER71 |
| C | LYS73 |
| C | HIS74 |
| C | GLY76 |
| C | HEZ234 |
| C | HOH445 |
| C | HOH505 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HEZ B 234 |
| Chain | Residue |
| B | GLN116 |
| B | GLY117 |
| B | GLN192 |
| B | PRO213 |
| B | HEZ236 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HEZ B 235 |
| Chain | Residue |
| A | GLN115 |
| B | ASP107 |
| B | VAL111 |
| B | LYS142 |
| B | HEZ237 |
| B | HOH273 |
| B | HOH586 |
| B | HOH644 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HEZ C 233 |
| Chain | Residue |
| C | GLN116 |
| C | VAL214 |
| C | HOH591 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HEZ D 233 |
| Chain | Residue |
| B | LYS73 |
| B | HIS74 |
| B | ALA75 |
| B | GLY76 |
| D | SER71 |
| D | HIS74 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE HEZ C 234 |
| Chain | Residue |
| A | HIS74 |
| C | HIS74 |
| C | ARG127 |
| C | GLN132 |
| C | HEZ232 |
| C | HOH241 |
| C | HOH705 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HEZ B 236 |
| Chain | Residue |
| B | GLY190 |
| B | VAL191 |
| B | GLN192 |
| B | HEZ233 |
| B | HEZ234 |
| B | HOH625 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE HEZ C 235 |
| Chain | Residue |
| C | GLN25 |
| C | HIS26 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HEZ B 237 |
| Chain | Residue |
| B | LEU102 |
| B | LEU103 |
| B | LYS142 |
| B | TYR228 |
| B | HEZ235 |
| B | HOH307 |
| B | HOH312 |
| B | HOH644 |
| B | HOH645 |
| site_id | BC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE HEZ B 238 |
| Chain | Residue |
| B | HIS26 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HEZ A 237 |
| Chain | Residue |
| A | LYS73 |
| A | HIS74 |
| A | ALA96 |
| A | ALA97 |
| A | CYS98 |
| A | HEZ236 |
| C | GLN189 |
| C | HOH509 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HEZ C 236 |
| Chain | Residue |
| C | ASP92 |
| C | ASP93 |
| C | ALA96 |
| C | HOH290 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HEZ B 239 |
| Chain | Residue |
| B | GLN116 |
| B | VAL214 |
| B | HOH482 |
| B | HOH594 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HEZ D 234 |
| Chain | Residue |
| B | ASP93 |
| B | GLN189 |
| D | ALA97 |
| D | CYS98 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HEZ D 235 |
| Chain | Residue |
| C | GLN115 |
| C | GLY117 |
| D | GLN112 |
| D | GLN116 |
| D | VAL214 |
| D | PHE215 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HEZ B 240 |
| Chain | Residue |
| B | MSE11 |
| B | THR86 |
| B | TYR163 |
Functional Information from PROSITE/UniProt
| site_id | PS00923 |
| Number of Residues | 10 |
| Details | ASP_GLU_RACEMASE_1 Aspartate and glutamate racemases signature 1. IVvCtNTMHK |
| Chain | Residue | Details |
| A | ILE80-LYS89 |
