5UMF
Crystal Structure of a Ribulose-phosphate 3-epimerase from Neisseria gonorrhoeae with bound phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| A | 0019323 | biological_process | pentose catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| B | 0019323 | biological_process | pentose catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006098 | biological_process | pentose-phosphate shunt |
| C | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| C | 0019323 | biological_process | pentose catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS34 |
| A | ASP36 |
| A | HIS67 |
| A | ASP180 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue PO4 A 302 |
| Chain | Residue |
| A | SER203 |
| A | HOH402 |
| A | HOH420 |
| A | HOH424 |
| A | HOH438 |
| A | HOH443 |
| A | HOH446 |
| A | GLY145 |
| A | GLY146 |
| A | GLY182 |
| A | ALA201 |
| A | GLY202 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | ASN24 |
| A | HOH555 |
| A | HOH567 |
| C | ASP107 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS34 |
| B | ASP36 |
| B | HIS67 |
| B | ASP180 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue PO4 B 302 |
| Chain | Residue |
| B | GLY146 |
| B | GLY182 |
| B | ALA201 |
| B | GLY202 |
| B | SER203 |
| B | HOH427 |
| B | HOH429 |
| B | HOH435 |
| B | HOH442 |
| B | HOH470 |
| B | HOH495 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | ASN24 |
| B | PRO209 |
| B | ASP210 |
| B | TYR211 |
| B | LYS212 |
| B | HOH471 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| A | ASP107 |
| B | ALA23 |
| B | ASN24 |
| B | HOH428 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | HIS34 |
| C | ASP36 |
| C | HIS67 |
| C | ASP180 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue PO4 C 302 |
| Chain | Residue |
| C | GLY145 |
| C | GLY146 |
| C | GLY182 |
| C | ALA201 |
| C | GLY202 |
| C | SER203 |
| C | HOH411 |
| C | HOH430 |
| C | HOH435 |
| C | HOH439 |
| C | HOH441 |
| C | HOH449 |
| C | HOH482 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 303 |
| Chain | Residue |
| B | ASP107 |
| B | MET108 |
| C | ASN24 |
| C | HOH452 |
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. IHFDVmDnhYVpNlT |
| Chain | Residue | Details |
| A | ILE33-THR47 |
| site_id | PS01086 |
| Number of Residues | 23 |
| Details | RIBUL_P_3_EPIMER_2 Ribulose-phosphate 3-epimerase family signature 2. VlLMSVnPgfgGQsFiphtleKI |
| Chain | Residue | Details |
| A | VAL135-ILE157 |
