5NC9
Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue 8SZ A 301 |
| Chain | Residue |
| A | ASP76 |
| D | HIS269 |
| A | ASP77 |
| A | HIS126 |
| A | HIS130 |
| A | PRO166 |
| A | TYR167 |
| A | HIS230 |
| A | HIS233 |
| A | ZN302 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | ASP77 |
| A | HIS126 |
| A | HIS130 |
| A | 8SZ301 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue 8SZ B 301 |
| Chain | Residue |
| B | ASP76 |
| B | ASP77 |
| B | HIS126 |
| B | HIS130 |
| B | PRO166 |
| B | TYR167 |
| B | TRP198 |
| B | HIS230 |
| B | ZN302 |
| B | HOH417 |
| B | HOH418 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | ASP77 |
| B | HIS126 |
| B | HIS130 |
| B | 8SZ301 |
| B | HOH417 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CIT B 303 |
| Chain | Residue |
| B | TRP191 |
| B | THR192 |
| B | ASP194 |
| B | ASN219 |
| B | PHE267 |
| C | MET170 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| A | ARG272 |
| B | GLU85 |
| B | PRO234 |
| B | HOH401 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue 8SZ C 301 |
| Chain | Residue |
| B | HIS269 |
| C | ASP76 |
| C | ASP77 |
| C | HIS126 |
| C | HIS130 |
| C | PRO166 |
| C | TYR167 |
| C | HIS230 |
| C | HIS233 |
| C | ZN302 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 302 |
| Chain | Residue |
| C | ASP77 |
| C | HIS126 |
| C | HIS130 |
| C | 8SZ301 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue 8SZ D 301 |
| Chain | Residue |
| D | ASP76 |
| D | ASP77 |
| D | HIS126 |
| D | HIS130 |
| D | PRO166 |
| D | TYR167 |
| D | TRP191 |
| D | TRP198 |
| D | HIS230 |
| D | ZN302 |
| D | HOH412 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 302 |
| Chain | Residue |
| D | ASP77 |
| D | HIS126 |
| D | HIS130 |
| D | 8SZ301 |
| D | HOH412 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue PGE D 303 |
| Chain | Residue |
| B | LEU196 |
| B | ARG199 |
| B | TYR200 |
| D | ARG199 |
| D | TYR200 |
| D | ASN201 |
| D | LYS202 |
| D | MET203 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 744 |
| Details | Domain: {"description":"NodB homology","evidences":[{"source":"PROSITE-ProRule","id":"PRU01014","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"29257674","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"29257674","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29257674","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
