5NCD
Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide
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 | 8 |
| Details | binding site for residue ACT A 301 |
| Chain | Residue |
| A | ASP76 |
| A | HIS126 |
| A | HIS130 |
| A | PRO166 |
| A | TYR167 |
| A | HIS230 |
| A | ZN302 |
| D | HIS269 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | HIS126 |
| A | HIS130 |
| A | ACT301 |
| A | HOH431 |
| A | ASP77 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue AHL B 301 |
| Chain | Residue |
| B | ASP76 |
| B | ASP77 |
| B | HIS126 |
| B | HIS130 |
| B | PRO166 |
| B | TYR167 |
| B | LEU228 |
| B | HIS230 |
| B | ZN302 |
| B | HOH423 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | ASP77 |
| B | HIS126 |
| B | HIS130 |
| B | AHL301 |
| B | HOH423 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CIT B 303 |
| Chain | Residue |
| B | TRP191 |
| B | THR192 |
| B | ILE193 |
| B | ASN219 |
| B | PHE267 |
| C | MET170 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue ACT C 301 |
| Chain | Residue |
| B | HIS269 |
| C | ASP76 |
| C | HIS126 |
| C | HIS130 |
| C | TYR167 |
| C | HIS230 |
| C | ZN302 |
| C | HOH415 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 302 |
| Chain | Residue |
| C | ASP77 |
| C | HIS126 |
| C | HIS130 |
| C | ACT301 |
| C | HOH415 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue ACT D 301 |
| Chain | Residue |
| D | ASP76 |
| D | HIS126 |
| D | HIS130 |
| D | PRO166 |
| D | TYR167 |
| D | HIS230 |
| D | ZN302 |
| D | HOH412 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 302 |
| Chain | Residue |
| D | ASP77 |
| D | HIS126 |
| D | HIS130 |
| D | ACT301 |
| D | HOH412 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:29257674 |
| Chain | Residue | Details |
| A | ASP76 | |
| B | ASP76 | |
| C | ASP76 | |
| D | ASP76 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:29257674 |
| Chain | Residue | Details |
| A | HIS230 | |
| B | HIS230 | |
| C | HIS230 | |
| D | HIS230 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29257674 |
| Chain | Residue | Details |
| B | HIS126 | |
| B | HIS130 | |
| C | ASP77 | |
| C | HIS126 | |
| C | HIS130 | |
| D | ASP77 | |
| D | HIS126 | |
| D | HIS130 | |
| A | ASP77 | |
| A | HIS126 | |
| A | HIS130 | |
| B | ASP77 |
