2DWU
Crystal Structure of Glutamate Racemase Isoform RacE1 from Bacillus anthracis
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 | 0042802 | molecular_function | identical protein binding |
| A | 0047661 | molecular_function | amino-acid racemase activity |
| 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 | 0042802 | molecular_function | identical protein binding |
| B | 0047661 | molecular_function | amino-acid racemase activity |
| B | 0071555 | biological_process | cell wall organization |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0008881 | molecular_function | glutamate racemase activity |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0047661 | molecular_function | amino-acid racemase activity |
| C | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 277 |
| Chain | Residue |
| B | TYR164 |
| B | HOH452 |
| C | THR242 |
| C | VAL265 |
| C | ASP266 |
| C | HOH313 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 277 |
| Chain | Residue |
| B | HOH309 |
| C | TYR164 |
| C | HOH396 |
| B | THR242 |
| B | VAL265 |
| B | ASP266 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 277 |
| Chain | Residue |
| A | TYR164 |
| A | THR242 |
| A | VAL265 |
| A | ASP266 |
| A | HOH320 |
| A | HOH394 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGL C 278 |
| Chain | Residue |
| C | ASP14 |
| C | SER15 |
| C | PRO45 |
| C | TYR46 |
| C | GLY47 |
| C | CYS77 |
| C | ASN78 |
| C | THR79 |
| C | THR121 |
| C | CYS188 |
| C | THR189 |
| C | HOH280 |
| C | HOH281 |
| C | HOH282 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGL B 278 |
| Chain | Residue |
| B | ASP14 |
| B | SER15 |
| B | PRO45 |
| B | TYR46 |
| B | GLY47 |
| B | CYS77 |
| B | ASN78 |
| B | THR79 |
| B | THR121 |
| B | CYS188 |
| B | THR189 |
| B | HOH281 |
| B | HOH282 |
| B | HOH283 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGL A 278 |
| Chain | Residue |
| A | ASP14 |
| A | SER15 |
| A | PRO45 |
| A | TYR46 |
| A | GLY47 |
| A | CYS77 |
| A | ASN78 |
| A | THR79 |
| A | THR121 |
| A | CYS188 |
| A | THR189 |
| A | HOH280 |
| A | HOH281 |
| A | HOH282 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL C 279 |
| Chain | Residue |
| C | VAL9 |
| C | LYS178 |
| C | GLU179 |
| C | ASP180 |
| C | ARG238 |
| C | HOH300 |
| C | HOH335 |
| C | HOH385 |
| C | HOH415 |
| C | HOH608 |
| C | HOH680 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 279 |
| Chain | Residue |
| B | VAL9 |
| B | SER34 |
| B | LYS178 |
| B | GLU179 |
| B | ASP180 |
| B | HOH317 |
| B | HOH379 |
| B | HOH381 |
| B | HOH401 |
| B | HOH599 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 279 |
| Chain | Residue |
| A | VAL9 |
| A | SER34 |
| A | HIS144 |
| A | GLU179 |
| A | ASP180 |
| A | HOH301 |
| A | HOH324 |
| A | HOH658 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 280 |
| Chain | Residue |
| B | HIS101 |
| B | MET129 |
| B | LYS132 |
| B | ALA133 |
| B | GLU136 |
| B | HOH544 |
Functional Information from PROSITE/UniProt
| site_id | PS00924 |
| Number of Residues | 11 |
| Details | ASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. LIlGCTHYPlL |
| Chain | Residue | Details |
| A | LEU184-LEU194 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1b73 |
| Chain | Residue | Details |
| A | SER15 | |
| A | ASP14 | |
| A | CYS77 | |
| A | CYS188 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1b73 |
| Chain | Residue | Details |
| C | SER15 | |
| C | ASP14 | |
| C | CYS77 | |
| C | CYS188 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1b73 |
| Chain | Residue | Details |
| B | SER15 | |
| B | ASP14 | |
| B | CYS77 | |
| B | CYS188 |
