6VLC
Crystal structure of UDP-GlcNAc 2-epimerase from Neisseria meningitidis bound to UDP-GlcNAc
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue UD1 A 400 |
| Chain | Residue |
| A | ARG10 |
| A | ARG135 |
| A | HIS212 |
| A | GLN270 |
| A | TYR272 |
| A | PHE275 |
| A | SER289 |
| A | GLY290 |
| A | GLY291 |
| A | GLU295 |
| A | ARG312 |
| A | PRO11 |
| A | HOH505 |
| A | HOH509 |
| A | HOH549 |
| A | HOH555 |
| A | HOH585 |
| A | HOH597 |
| A | HOH614 |
| A | HOH633 |
| A | GLU12 |
| A | LYS15 |
| A | HIS93 |
| A | ASP95 |
| A | THR96 |
| A | GLU117 |
| A | PRO128 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | binding site for residue UD1 C 400 |
| Chain | Residue |
| C | ARG10 |
| C | PRO11 |
| C | GLU12 |
| C | LYS15 |
| C | HIS93 |
| C | ASP95 |
| C | GLU117 |
| C | ARG135 |
| C | HIS212 |
| C | GLN270 |
| C | TYR272 |
| C | PHE275 |
| C | MET279 |
| C | SER289 |
| C | GLY290 |
| C | GLY291 |
| C | GLU295 |
| C | ARG312 |
| C | HOH501 |
| C | HOH522 |
| C | HOH527 |
| C | HOH531 |
| C | HOH557 |
| C | HOH573 |
| C | HOH577 |
| C | HOH610 |
| C | HOH618 |
| C | HOH634 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P27828 |
| Chain | Residue | Details |
| A | ARG10 | |
| A | ARG312 | |
| B | ARG10 | |
| B | LYS15 | |
| B | ASP95 | |
| B | GLU117 | |
| B | HIS212 | |
| B | GLN270 | |
| B | PHE275 | |
| B | SER289 | |
| B | GLU295 | |
| A | LYS15 | |
| B | ARG312 | |
| C | ARG10 | |
| C | LYS15 | |
| C | ASP95 | |
| C | GLU117 | |
| C | HIS212 | |
| C | GLN270 | |
| C | PHE275 | |
| C | SER289 | |
| C | GLU295 | |
| A | ASP95 | |
| C | ARG312 | |
| D | ARG10 | |
| D | LYS15 | |
| D | ASP95 | |
| D | GLU117 | |
| D | HIS212 | |
| D | GLN270 | |
| D | PHE275 | |
| D | SER289 | |
| D | GLU295 | |
| A | GLU117 | |
| D | ARG312 | |
| A | HIS212 | |
| A | GLN270 | |
| A | PHE275 | |
| A | SER289 | |
| A | GLU295 |
