5GM3
Crystal structure of FI-CMCase from Aspergillus aculeatus F-50
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005576 | cellular_component | extracellular region |
A | 0008810 | molecular_function | cellulase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0030245 | biological_process | cellulose catabolic process |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005576 | cellular_component | extracellular region |
B | 0008810 | molecular_function | cellulase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0030245 | biological_process | cellulose catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue ZN A 301 |
Chain | Residue |
A | HIS185 |
A | CAC306 |
A | CAC306 |
A | CAC307 |
A | CAC307 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue ZN A 302 |
Chain | Residue |
A | HOH425 |
A | HOH651 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ZN A 303 |
Chain | Residue |
B | ASP107 |
B | HOH419 |
B | HOH615 |
A | ASP7 |
A | HOH577 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue ZN A 304 |
Chain | Residue |
A | ASP116 |
A | HOH605 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue ZN A 305 |
Chain | Residue |
A | HIS110 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue CAC A 306 |
Chain | Residue |
A | ASN184 |
A | HIS185 |
A | HIS185 |
A | ZN301 |
A | ZN301 |
A | CAC307 |
A | CAC307 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue CAC A 307 |
Chain | Residue |
A | TYR150 |
A | TYR159 |
A | HIS185 |
A | HIS185 |
A | ZN301 |
A | ZN301 |
A | CAC306 |
A | CAC306 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | HIS185 |
B | CAC304 |
B | CAC304 |
B | CAC305 |
B | CAC305 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue ZN B 302 |
Chain | Residue |
B | HIS110 |
B | HOH507 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue ZN B 303 |
Chain | Residue |
B | ASP116 |
B | HOH633 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue CAC B 304 |
Chain | Residue |
B | ASN184 |
B | HIS185 |
B | HIS185 |
B | ZN301 |
B | ZN301 |
B | CAC305 |
B | CAC305 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue CAC B 305 |
Chain | Residue |
B | TYR150 |
B | TYR159 |
B | HIS185 |
B | HIS185 |
B | ZN301 |
B | ZN301 |
B | CAC304 |
B | CAC304 |