3EGJ
N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| A | 0006046 | biological_process | N-acetylglucosamine catabolic process |
| A | 0008448 | molecular_function | N-acetylglucosamine-6-phosphate deacetylase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| B | 0006046 | biological_process | N-acetylglucosamine catabolic process |
| B | 0008448 | molecular_function | N-acetylglucosamine-6-phosphate deacetylase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI A 401 |
| Chain | Residue |
| A | GLU128 |
| A | HIS140 |
| A | HIS192 |
| A | HIS213 |
| B | HOH405 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI B 402 |
| Chain | Residue |
| B | GLU128 |
| B | HIS192 |
| B | HIS213 |
| B | HOH406 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | ARG224 |
| B | PHE215 |
| B | ASN216 |
| B | ALA217 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 404 |
| Chain | Residue |
| A | ASN216 |
| A | ALA217 |
| B | ARG224 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P0AF18","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2009","submissionDatabase":"PDB data bank","title":"X-ray crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate.","authoringGroup":["Center for structural genomics of infectious diseases (CSGID)"]}}]} |
| Chain | Residue | Details |
