5ZJB
Structure of N-acetylmannosamine-6-phosphate-2-epimerase from Vibrio cholerae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003674 | molecular_function | molecular_function |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006051 | biological_process | N-acetylmannosamine metabolic process |
| A | 0006053 | biological_process | N-acetylmannosamine catabolic process |
| A | 0008150 | biological_process | biological_process |
| A | 0009385 | molecular_function | N-acylmannosamine-6-phosphate 2-epimerase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| A | 0047465 | molecular_function | N-acylglucosamine-6-phosphate 2-epimerase activity |
| B | 0003674 | molecular_function | molecular_function |
| B | 0005575 | cellular_component | cellular_component |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006051 | biological_process | N-acetylmannosamine metabolic process |
| B | 0006053 | biological_process | N-acetylmannosamine catabolic process |
| B | 0008150 | biological_process | biological_process |
| B | 0009385 | molecular_function | N-acylmannosamine-6-phosphate 2-epimerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| B | 0047465 | molecular_function | N-acylglucosamine-6-phosphate 2-epimerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue MLI A 301 |
| Chain | Residue |
| A | ARG188 |
| A | HOH468 |
| A | GLY209 |
| A | SER210 |
| A | ARG214 |
| A | HOH408 |
| A | HOH410 |
| A | HOH452 |
| A | HOH457 |
| A | HOH467 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 302 |
| Chain | Residue |
| A | GLN46 |
| A | HOH522 |
| B | GLY28 |
| B | SER29 |
| B | PRO30 |
| B | GLU216 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 303 |
| Chain | Residue |
| A | TRP221 |
| B | HOH419 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 304 |
| Chain | Residue |
| A | GLY100 |
| A | THR102 |
| A | HOH402 |
| A | HOH444 |
| A | HOH481 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue MLI B 301 |
| Chain | Residue |
| B | ARG188 |
| B | GLY209 |
| B | SER210 |
| B | ARG214 |
| B | MLI302 |
| B | HOH411 |
| B | HOH420 |
| B | HOH424 |
| B | HOH443 |
| B | HOH446 |
| B | HOH462 |
| B | HOH479 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue MLI B 302 |
| Chain | Residue |
| B | LYS76 |
| B | ARG85 |
| B | ILE86 |
| B | TYR159 |
| B | MLI301 |
| B | HOH410 |
| B | HOH420 |
| B | HOH443 |
| B | HOH502 |
| B | HOH540 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 303 |
| Chain | Residue |
| B | THR191 |
| B | GLU193 |
| B | LEU194 |
| B | HOH503 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue PEG B 304 |
| Chain | Residue |
| A | GLU193 |
| B | THR191 |
| B | TRP221 |
