4NU7
2.05 Angstrom Crystal Structure of Ribulose-phosphate 3-epimerase from Toxoplasma gondii.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| B | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| C | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006098 | biological_process | pentose-phosphate shunt |
| C | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| D | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0006098 | biological_process | pentose-phosphate shunt |
| D | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 301 |
| Chain | Residue |
| A | HIS44 |
| C | HOH496 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | ARG112 |
| A | SO4308 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 303 |
| Chain | Residue |
| A | HIS37 |
| A | ASP39 |
| A | HIS71 |
| A | ASP182 |
| A | HOH434 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 304 |
| Chain | Residue |
| A | GLY155 |
| A | GLY156 |
| A | GLY183 |
| A | GLY184 |
| A | GLY204 |
| A | THR205 |
| A | HOH410 |
| A | HOH423 |
| A | HOH508 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 305 |
| Chain | Residue |
| A | GLU97 |
| A | LYS125 |
| A | HOH418 |
| A | HOH479 |
| B | HIS44 |
| D | HIS44 |
| D | SER75 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 306 |
| Chain | Residue |
| A | THR218 |
| A | ARG221 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 307 |
| Chain | Residue |
| A | ARG112 |
| C | LYS191 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 308 |
| Chain | Residue |
| A | ARG112 |
| A | ARG116 |
| A | CL302 |
| A | HOH430 |
| A | HOH527 |
| C | GLY187 |
| C | GLU188 |
| C | HOH478 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 301 |
| Chain | Residue |
| B | GLU188 |
| D | ARG112 |
| D | ARG116 |
| D | HOH492 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 302 |
| Chain | Residue |
| B | ALA85 |
| B | ARG116 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 303 |
| Chain | Residue |
| B | HIS37 |
| B | ASP39 |
| B | HIS71 |
| B | ASP182 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 B 304 |
| Chain | Residue |
| B | GLY155 |
| B | GLY156 |
| B | GLY183 |
| B | GLY184 |
| B | GLY204 |
| B | THR205 |
| B | HOH409 |
| B | HOH415 |
| B | HOH495 |
| B | HOH502 |
| B | HOH509 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 305 |
| Chain | Residue |
| B | ILE81 |
| B | ARG112 |
| B | ARG116 |
| B | HOH437 |
| B | HOH445 |
| C | LYS79 |
| C | GLN82 |
| C | PRO83 |
| C | HOH441 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 306 |
| Chain | Residue |
| B | THR218 |
| B | ARG221 |
| B | HOH465 |
| B | HOH473 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 301 |
| Chain | Residue |
| C | THR218 |
| C | ARG221 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 302 |
| Chain | Residue |
| C | HIS37 |
| C | ASP39 |
| C | HIS71 |
| C | ASP182 |
| C | HOH513 |
| site_id | BC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 C 303 |
| Chain | Residue |
| C | GLY155 |
| C | GLY156 |
| C | GLY183 |
| C | GLY184 |
| C | GLY204 |
| C | THR205 |
| C | HOH403 |
| C | HOH422 |
| C | HOH426 |
| C | HOH429 |
| C | HOH506 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 304 |
| Chain | Residue |
| A | HIS44 |
| C | HIS44 |
| C | SER75 |
| C | HOH451 |
| C | HOH489 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| D | HIS37 |
| D | ASP39 |
| D | HIS71 |
| D | ASP182 |
| D | HOH527 |
| site_id | CC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 D 302 |
| Chain | Residue |
| D | GLY155 |
| D | GLY156 |
| D | GLY183 |
| D | GLY184 |
| D | GLY204 |
| D | THR205 |
| D | HOH417 |
| D | HOH468 |
| D | HOH483 |
| D | HOH502 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 303 |
| Chain | Residue |
| D | THR218 |
| D | ARG221 |
| D | HOH485 |
Functional Information from PROSITE/UniProt
| site_id | PS01085 |
| Number of Residues | 15 |
| Details | RIBUL_P_3_EPIMER_1 Ribulose-phosphate 3-epimerase family signature 1. LHLDImDghFVpNiS |
| Chain | Residue | Details |
| A | LEU36-SER50 |
| site_id | PS01086 |
| Number of Residues | 23 |
| Details | RIBUL_P_3_EPIMER_2 Ribulose-phosphate 3-epimerase family signature 2. LlVMTVePgfgGQkFmadmlqKV |
| Chain | Residue | Details |
| A | LEU145-VAL167 |
