6ZT6
X-ray structure of mutated arabinofuranosidase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0046373 | biological_process | L-arabinose metabolic process |
A | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0046373 | biological_process | L-arabinose metabolic process |
B | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
C | 0046373 | biological_process | L-arabinose metabolic process |
C | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue MPD A 501 |
Chain | Residue |
A | ASP260 |
A | LYS267 |
A | GLU396 |
A | GLU398 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue MPD A 502 |
Chain | Residue |
A | TYR286 |
A | HOH644 |
C | GLU224 |
C | HOH741 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue MPD A 503 |
Chain | Residue |
A | GLY73 |
A | CYS74 |
A | GLU176 |
A | TYR242 |
A | LEU314 |
A | GLN347 |
A | GLU28 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue MPD A 504 |
Chain | Residue |
A | CYS122 |
A | ARG167 |
A | HOH725 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue MPD A 505 |
Chain | Residue |
A | LYS15 |
A | ARG335 |
A | ASP338 |
A | HOH782 |
A | HOH1039 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MPD A 506 |
Chain | Residue |
A | PRO232 |
A | PHE233 |
A | MET234 |
A | HIS235 |
A | HOH983 |
A | HOH1000 |
site_id | AC7 |
Number of Residues | 15 |
Details | binding site for residue BTB A 507 |
Chain | Residue |
A | GLY86 |
A | PRO87 |
A | ARG88 |
A | ARG91 |
A | GLU112 |
A | ASN160 |
A | HOH608 |
A | HOH653 |
A | HOH703 |
A | HOH825 |
A | HOH865 |
C | GLU42 |
C | ASP43 |
C | ARG88 |
C | GLU89 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue MPD B 501 |
Chain | Residue |
B | LYS15 |
B | ARG335 |
B | ASP338 |
B | HOH690 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue MPD B 502 |
Chain | Residue |
B | ASP260 |
B | TRP263 |
B | PRO395 |
B | GLU398 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue MPD B 503 |
Chain | Residue |
B | TYR220 |
B | TYR286 |
B | HOH761 |
B | HOH995 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue MPD B 504 |
Chain | Residue |
B | GLU28 |
B | LEU30 |
B | GLY73 |
B | CYS74 |
B | GLU176 |
B | TYR242 |
B | GLU298 |
B | HOH890 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue MPD B 505 |
Chain | Residue |
B | PRO232 |
B | PHE233 |
B | MET234 |
B | HIS235 |
B | ARG291 |
B | HOH928 |
B | HOH975 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue MPD C 501 |
Chain | Residue |
A | TYR220 |
A | GLU224 |
C | TYR286 |
C | HOH662 |
C | HOH956 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue MPD C 502 |
Chain | Residue |
C | GLU28 |
C | LEU30 |
C | CYS74 |
C | GLU176 |
C | TYR242 |
C | GLU298 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue MPD C 503 |
Chain | Residue |
C | LYS15 |
C | ARG335 |
C | ASP338 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue MPD C 504 |
Chain | Residue |
C | LYS210 |
C | PRO232 |
C | PHE233 |
C | MET234 |
C | HIS235 |
C | HOH932 |