4XM1
N,N'-diacetylchitobiose deacetylase from Pyrococcus furiosus in the presence of cadmium
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
A | 0046872 | molecular_function | metal ion binding |
B | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
B | 0046872 | molecular_function | metal ion binding |
C | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
C | 0046872 | molecular_function | metal ion binding |
D | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
D | 0046872 | molecular_function | metal ion binding |
E | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
E | 0046872 | molecular_function | metal ion binding |
F | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CD A 301 |
Chain | Residue |
A | HIS40 |
A | ASP43 |
A | HIS151 |
A | GOL305 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CD A 302 |
Chain | Residue |
A | GLU225 |
A | CL304 |
C | MET1 |
C | CL303 |
C | CL304 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue HEZ A 303 |
Chain | Residue |
A | TYR116 |
A | PHE156 |
B | HEZ302 |
C | HEZ302 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CL A 304 |
Chain | Residue |
A | GLU225 |
A | CD302 |
C | CL304 |
F | PHE2 |
F | ASN4 |
F | VAL5 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | ASP42 |
A | ASP43 |
A | ILE46 |
A | HIS151 |
A | CD301 |
C | HIS259 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CD B 301 |
Chain | Residue |
B | HIS40 |
B | ASP43 |
B | HIS151 |
B | HOH444 |
B | HOH445 |
B | HOH447 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue HEZ B 302 |
Chain | Residue |
A | HEZ303 |
B | PHE156 |
B | HOH456 |
C | PRO141 |
C | HEZ302 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CD C 301 |
Chain | Residue |
B | HOH442 |
B | HOH443 |
C | HIS40 |
C | ASP43 |
C | HIS151 |
C | HOH459 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue HEZ C 302 |
Chain | Residue |
A | PRO141 |
A | HEZ303 |
A | HOH478 |
B | HEZ302 |
C | HOH452 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue CL C 303 |
Chain | Residue |
A | CD302 |
F | MET1 |
F | PHE2 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue CL C 304 |
Chain | Residue |
A | CD302 |
A | CL304 |
C | MET1 |
F | PHE2 |
F | GLU3 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue CD D 301 |
Chain | Residue |
D | HIS40 |
D | ASP43 |
D | HIS151 |
D | GOL305 |
F | HOH446 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue CD D 302 |
Chain | Residue |
D | GLU225 |
D | CL304 |
F | MET1 |
F | CL303 |
F | CL304 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue HEZ D 303 |
Chain | Residue |
D | PRO141 |
D | ARG152 |
D | HOH428 |
E | HEZ302 |
F | PHE156 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue CL D 304 |
Chain | Residue |
C | ASN4 |
C | LYS14 |
D | GLU225 |
D | CD302 |
F | CL304 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue GOL D 305 |
Chain | Residue |
D | ASP42 |
D | ASP43 |
D | HIS151 |
D | CD301 |
F | HIS259 |
F | ILE260 |
F | HOH446 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue CD E 301 |
Chain | Residue |
E | HIS40 |
E | ASP43 |
E | HIS151 |
E | HOH437 |
site_id | AD9 |
Number of Residues | 7 |
Details | binding site for residue HEZ E 302 |
Chain | Residue |
D | PHE156 |
D | HEZ303 |
E | PRO141 |
E | ARG152 |
E | HOH427 |
E | HOH442 |
F | HEZ302 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue CD F 301 |
Chain | Residue |
E | HOH435 |
E | HOH436 |
F | HIS40 |
F | ASP43 |
F | HIS151 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue HEZ F 302 |
Chain | Residue |
E | HEZ302 |
F | ARG152 |
F | HOH404 |
F | HOH438 |
E | PHE156 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue CL F 303 |
Chain | Residue |
C | MET1 |
C | PHE2 |
D | CD302 |
F | MET1 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue CL F 304 |
Chain | Residue |
C | GLU3 |
D | CD302 |
D | CL304 |
F | MET1 |