5N1J
Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | ASP77 |
| A | HIS126 |
| A | HIS130 |
| A | ACT302 |
| A | HOH417 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue ACT A 302 |
| Chain | Residue |
| A | PRO166 |
| A | TYR167 |
| A | TRP191 |
| A | HIS230 |
| A | ZN301 |
| A | HOH417 |
| A | ASP76 |
| A | ASP77 |
| A | HIS126 |
| A | HIS130 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | LYS146 |
| A | GLN149 |
| A | GLY150 |
| A | SER159 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | HIS269 |
| A | ASP270 |
| A | ASN271 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | ASP77 |
| B | HIS126 |
| B | HIS130 |
| B | ACT302 |
| B | HOH416 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue ACT B 302 |
| Chain | Residue |
| B | ASP76 |
| B | ASP77 |
| B | HIS126 |
| B | HIS130 |
| B | PRO166 |
| B | TYR167 |
| B | HIS230 |
| B | ZN301 |
| B | HOH416 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | THR192 |
| B | ILE193 |
| B | ASP194 |
| B | HOH474 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | ARG199 |
| B | TYR200 |
| B | ASN201 |
| B | LYS202 |
| B | MET203 |
| D | ARG199 |
| D | TYR200 |
| D | HOH457 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | TRP191 |
| B | VAL265 |
| B | ASN266 |
| B | HOH461 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | ASP77 |
| C | HIS126 |
| C | HIS130 |
| C | ACT302 |
| C | HOH403 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue ACT C 302 |
| Chain | Residue |
| C | ASP76 |
| C | ASP77 |
| C | HIS126 |
| C | HIS130 |
| C | PRO166 |
| C | TYR167 |
| C | HIS230 |
| C | ZN301 |
| C | HOH403 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | ASP77 |
| D | HIS126 |
| D | HIS130 |
| D | ACT302 |
| D | HOH408 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue ACT D 302 |
| Chain | Residue |
| D | ASP76 |
| D | ASP77 |
| D | HIS126 |
| D | HIS130 |
| D | PRO166 |
| D | TYR167 |
| D | HIS230 |
| D | ZN301 |
| D | HOH408 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| D | GLU147 |
| D | HOH431 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 304 |
| Chain | Residue |
| D | GLU85 |
| D | PRO234 |
| D | HOH430 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 305 |
| Chain | Residue |
| B | ARG199 |
| B | TYR200 |
| D | ARG199 |
| D | TYR200 |
| D | ASN201 |
| D | LYS202 |
| D | MET203 |
| D | HOH457 |
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 |
