3OJC
Crystal structure of a putative Asp/Glu Racemase from Yersinia pestis
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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 |