3OZM
Crystal structure of enolase superfamily member from Bordetella bronchiseptica complexed with Mg, m-Xylarate and L-Lyxarate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0009063 | biological_process | amino acid catabolic process |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0009063 | biological_process | amino acid catabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0009063 | biological_process | amino acid catabolic process |
| C | 0016052 | biological_process | carbohydrate catabolic process |
| C | 0016836 | molecular_function | hydro-lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0009063 | biological_process | amino acid catabolic process |
| D | 0016052 | biological_process | carbohydrate catabolic process |
| D | 0016836 | molecular_function | hydro-lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0009063 | biological_process | amino acid catabolic process |
| E | 0016052 | biological_process | carbohydrate catabolic process |
| E | 0016836 | molecular_function | hydro-lyase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0009063 | biological_process | amino acid catabolic process |
| F | 0016052 | biological_process | carbohydrate catabolic process |
| F | 0016836 | molecular_function | hydro-lyase activity |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0009063 | biological_process | amino acid catabolic process |
| G | 0016052 | biological_process | carbohydrate catabolic process |
| G | 0016836 | molecular_function | hydro-lyase activity |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0009063 | biological_process | amino acid catabolic process |
| H | 0016052 | biological_process | carbohydrate catabolic process |
| H | 0016836 | molecular_function | hydro-lyase activity |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 390 |
| Chain | Residue |
| A | ASP201 |
| A | GLU227 |
| A | GLU254 |
| A | DXL391 |
| A | HOH2283 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 390 |
| Chain | Residue |
| B | HOH2286 |
| B | ASP201 |
| B | GLU227 |
| B | GLU254 |
| B | DXL391 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 390 |
| Chain | Residue |
| C | ASP201 |
| C | GLU227 |
| C | GLU254 |
| C | DXL391 |
| C | HOH2285 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 390 |
| Chain | Residue |
| D | ASP201 |
| D | GLU227 |
| D | GLU254 |
| D | LY9391 |
| D | HOH2281 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 390 |
| Chain | Residue |
| E | ASP201 |
| E | GLU227 |
| E | GLU254 |
| E | DXL391 |
| E | HOH2287 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 390 |
| Chain | Residue |
| F | ASP201 |
| F | GLU227 |
| F | GLU254 |
| F | DXL391 |
| F | HOH399 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G 390 |
| Chain | Residue |
| G | ASP201 |
| G | GLU227 |
| G | GLU254 |
| G | DXL391 |
| G | HOH2284 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG H 390 |
| Chain | Residue |
| H | ASP201 |
| H | GLU227 |
| H | GLU254 |
| H | LY9391 |
| H | HOH2282 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DXL A 391 |
| Chain | Residue |
| A | SER25 |
| A | LYS30 |
| A | TYR147 |
| A | LYS171 |
| A | LYS173 |
| A | ASP201 |
| A | ASN203 |
| A | GLU227 |
| A | GLU254 |
| A | HIS304 |
| A | PHE306 |
| A | GLU329 |
| A | MG390 |
| site_id | BC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DXL B 391 |
| Chain | Residue |
| B | SER25 |
| B | LYS30 |
| B | TYR147 |
| B | LYS171 |
| B | LYS173 |
| B | ASP201 |
| B | ASN203 |
| B | GLU227 |
| B | GLU254 |
| B | HIS304 |
| B | PHE306 |
| B | GLU329 |
| B | MG390 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DXL C 391 |
| Chain | Residue |
| C | SER25 |
| C | LYS30 |
| C | TYR147 |
| C | LYS171 |
| C | LYS173 |
| C | ASP201 |
| C | ASN203 |
| C | GLU227 |
| C | GLU254 |
| C | HIS304 |
| C | PHE306 |
| C | GLU329 |
| C | MG390 |
| C | HOH735 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LY9 D 391 |
| Chain | Residue |
| D | LYS171 |
| D | LYS173 |
| D | ASP201 |
| D | ASN203 |
| D | GLU227 |
| D | GLU254 |
| D | HIS304 |
| D | PHE306 |
| D | GLU329 |
| D | MG390 |
| D | HOH839 |
| D | HOH2323 |
| site_id | BC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DXL E 391 |
| Chain | Residue |
| E | GLU227 |
| E | GLU254 |
| E | HIS304 |
| E | PHE306 |
| E | GLU329 |
| E | MG390 |
| E | HOH615 |
| E | SER25 |
| E | LYS30 |
| E | TYR147 |
| E | LYS171 |
| E | LYS173 |
| E | ASP201 |
| E | ASN203 |
| site_id | BC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DXL F 391 |
| Chain | Residue |
| F | SER25 |
| F | LYS30 |
| F | TYR147 |
| F | LYS171 |
| F | LYS173 |
| F | ASP201 |
| F | ASN203 |
| F | GLU227 |
| F | GLU254 |
| F | HIS304 |
| F | PHE306 |
| F | GLU329 |
| F | MG390 |
| site_id | BC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DXL G 391 |
| Chain | Residue |
| G | SER25 |
| G | LYS30 |
| G | TYR147 |
| G | LYS171 |
| G | LYS173 |
| G | ASP201 |
| G | ASN203 |
| G | GLU227 |
| G | GLU254 |
| G | HIS304 |
| G | PHE306 |
| G | GLU329 |
| G | MG390 |
| site_id | BC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LY9 H 391 |
| Chain | Residue |
| H | LYS30 |
| H | LYS171 |
| H | LYS173 |
| H | ASP201 |
| H | ASN203 |
| H | GLU227 |
| H | GLU254 |
| H | HIS304 |
| H | PHE306 |
| H | GLU329 |
| H | MG390 |
| H | HOH1449 |
| H | HOH2297 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL E 392 |
| Chain | Residue |
| E | THR47 |
| E | ARG120 |
| E | GLU364 |
| E | ILE365 |
| E | TRP367 |
| E | HOH2125 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 392 |
| Chain | Residue |
| C | GLU197 |
| C | GLY222 |
| C | CYS223 |
| C | PRO247 |
| C | ARG249 |
| C | HOH435 |
| C | HOH723 |
| C | HOH903 |
| site_id | CC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 392 |
| Chain | Residue |
| B | HOH644 |
| D | GLU197 |
| D | GLY222 |
| D | CYS223 |
| D | TYR224 |
| D | PRO247 |
| D | ARG249 |
| D | HOH403 |
| D | HOH621 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL H 392 |
| Chain | Residue |
| H | GLU197 |
| H | GLY222 |
| H | CYS223 |
| H | TYR224 |
| H | PRO247 |
| H | ARG249 |
| H | HOH430 |
| H | HOH433 |
| H | HOH647 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL G 392 |
| Chain | Residue |
| G | HIS86 |
| G | PHE89 |
| G | HIS90 |
| G | ARG259 |
| G | ASN260 |
| G | GLU286 |
| G | HOH2017 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 393 |
| Chain | Residue |
| C | ASP57 |
| C | HOH693 |
| C | HOH1109 |
| E | ARG63 |
| E | GLU92 |
| E | HOH636 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 392 |
| Chain | Residue |
| B | HIS86 |
| B | HIS90 |
| B | ARG259 |
| B | ASN260 |
| B | GLU286 |
| B | HOH1475 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 393 |
| Chain | Residue |
| B | ARG63 |
| B | ASP67 |
| B | GLU92 |
| B | HOH806 |
| B | HOH1344 |
| B | HOH1728 |
| H | ASP57 |
| site_id | CC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 394 |
| Chain | Residue |
| C | ASP67 |
| C | VAL68 |
| C | GLU92 |
| C | HOH1340 |
| C | HOH2249 |
| E | ASP57 |
| E | ILE381 |
| E | HOH2216 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 392 |
| Chain | Residue |
| A | THR47 |
| A | VAL49 |
| A | ARG120 |
| A | GLU364 |
| A | ILE365 |
| A | TRP367 |
Functional Information from PROSITE/UniProt
| site_id | PS00908 |
| Number of Residues | 26 |
| Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AmSGVDiALwDLkGRamnqPIyqLLG |
| Chain | Residue | Details |
| A | ALA106-GLY131 |
