1YRR
Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution
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 | 0008270 | molecular_function | zinc ion binding |
| 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 | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| 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 | 0008270 | molecular_function | zinc ion binding |
| 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 | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 501 |
| Chain | Residue |
| A | GLN59 |
| A | GLU131 |
| A | HIS195 |
| A | HIS216 |
| A | ASP273 |
| A | HOH858 |
| A | HOH860 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 502 |
| Chain | Residue |
| B | HIS195 |
| B | HIS216 |
| B | ASP273 |
| B | HOH672 |
| B | ASN61 |
| B | GLU131 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 601 |
| Chain | Residue |
| A | THR225 |
| A | GLY226 |
| A | ARG227 |
| A | GLU228 |
| B | TYR223 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 602 |
| Chain | Residue |
| A | ASP253 |
| A | ALA255 |
| A | ARG258 |
| A | HIS323 |
| A | HOH862 |
| A | HOH865 |
| A | HOH866 |
| B | LEU200 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 603 |
| Chain | Residue |
| A | LYS261 |
| A | ARG262 |
| A | GLY265 |
| A | HOH863 |
| A | HOH864 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17567048","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17567048","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
