5NC6
Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (E)-N-hydroxy-3-(naphthalen-1-yl)prop-2-enamide
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 | 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 ACT A 301 |
Chain | Residue |
A | ASP76 |
D | HIS269 |
A | ASP77 |
A | HIS126 |
A | HIS130 |
A | PRO166 |
A | TYR167 |
A | HIS230 |
A | ZN302 |
A | HOH403 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue ZN A 302 |
Chain | Residue |
A | ASP76 |
A | ASP77 |
A | HIS126 |
A | HIS130 |
A | ACT301 |
A | HOH403 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | ASP270 |
A | HOH402 |
B | GLU85 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue 8SQ B 301 |
Chain | Residue |
B | ASP76 |
B | ASP77 |
B | HIS126 |
B | HIS130 |
B | PRO166 |
B | TYR167 |
B | TRP198 |
B | HIS230 |
B | ZN302 |
B | HOH410 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue ZN B 302 |
Chain | Residue |
B | ASP77 |
B | HIS126 |
B | HIS130 |
B | 8SQ301 |
B | HOH410 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue ACT C 301 |
Chain | Residue |
B | HIS269 |
C | ASP76 |
C | ASP77 |
C | HIS126 |
C | HIS130 |
C | PRO166 |
C | TYR167 |
C | HIS230 |
C | ZN302 |
C | HOH408 |
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 | HOH408 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue 8SQ D 301 |
Chain | Residue |
D | ASP76 |
D | ASP77 |
D | HIS126 |
D | HIS130 |
D | PRO166 |
D | TYR167 |
D | ASP194 |
D | TRP198 |
D | ARG199 |
D | HIS230 |
D | ZN302 |
D | HOH401 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue ZN D 302 |
Chain | Residue |
D | ASP77 |
D | HIS126 |
D | HIS130 |
D | 8SQ301 |
D | HOH401 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue PGE D 303 |
Chain | Residue |
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 | 60 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
B | ILE10-ILE30 | |
C | ILE10-ILE30 | |
D | ILE10-ILE30 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:29257674 |
Chain | Residue | Details |
B | ASP76 | |
C | ASP76 | |
D | ASP76 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:29257674 |
Chain | Residue | Details |
B | HIS230 | |
C | HIS230 | |
D | HIS230 |
site_id | SWS_FT_FI4 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29257674 |
Chain | Residue | Details |
B | ASP77 | |
B | HIS126 | |
B | HIS130 | |
C | ASP77 | |
C | HIS126 | |
C | HIS130 | |
D | ASP77 | |
D | HIS126 | |
D | HIS130 |