7EFZ
Structure of Thermotoga maritima GH5 endoglucanase TM1752 in complex with TRIS
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 | 0008422 | molecular_function | beta-glucosidase activity |
A | 0009251 | biological_process | glucan catabolic process |
A | 0009986 | cellular_component | cell surface |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005576 | cellular_component | extracellular region |
B | 0008422 | molecular_function | beta-glucosidase activity |
B | 0009251 | biological_process | glucan catabolic process |
B | 0009986 | cellular_component | cell surface |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue TRS A 401 |
Chain | Residue |
A | HIS86 |
A | HOH677 |
A | GLU139 |
A | TYR200 |
A | HIS207 |
A | TRP212 |
A | GLU259 |
A | TRP292 |
A | HOH508 |
A | HOH529 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue IPA A 402 |
Chain | Residue |
A | ARG7 |
A | TRP8 |
A | HOH602 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue TRS B 401 |
Chain | Residue |
B | HIS86 |
B | GLU139 |
B | TYR200 |
B | HIS207 |
B | TRP212 |
B | GLU259 |
B | TRP292 |
B | HOH566 |
B | HOH669 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue IPA B 402 |
Chain | Residue |
A | ASP68 |
A | PHE72 |
A | ILE127 |
B | LYS76 |
B | HOH511 |
B | HOH549 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue IPA B 403 |
Chain | Residue |
B | PRO6 |
B | TRP8 |
B | HOH546 |