3AKT
Crystal structure of xylanase from Trichoderma longibrachiatum
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
A | 0045493 | biological_process | xylan catabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
B | 0045493 | biological_process | xylan catabolic process |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 191 |
Chain | Residue |
A | TRP18 |
A | HOH293 |
A | HOH344 |
A | ASN44 |
A | GLU86 |
A | TYR88 |
A | GLU177 |
A | GOL192 |
A | HOH198 |
A | HOH218 |
A | HOH247 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 192 |
Chain | Residue |
A | TYR77 |
A | TYR171 |
A | GOL191 |
A | HOH213 |
A | HOH247 |
A | HOH276 |
A | HOH308 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 191 |
Chain | Residue |
B | TRP18 |
B | ASN44 |
B | GLU86 |
B | TYR88 |
B | GLU177 |
B | HOH234 |
B | HOH278 |
B | HOH286 |
B | HOH302 |
B | HOH397 |
Functional Information from PROSITE/UniProt
site_id | PS00776 |
Number of Residues | 11 |
Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYIVEnF |
Chain | Residue | Details |
A | PRO83-PHE93 |
site_id | PS00777 |
Number of Residues | 12 |
Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. VavEGYFSSGsA |
Chain | Residue | Details |
A | VAL174-ALA185 |