3KST
Crystal structure of Endo-1,4-beta-xylanase (NP_811807.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.70 A resolution
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 | 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 | 0045493 | biological_process | xylan catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 400 |
| Chain | Residue |
| A | HOH8 |
| A | GLU107 |
| A | HIS275 |
| A | HOH389 |
| A | HOH397 |
| A | HOH398 |
| A | HOH399 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 400 |
| Chain | Residue |
| B | HOH20 |
| B | GLU107 |
| B | HIS275 |
| B | HOH437 |
| B | HOH568 |
| B | HOH2 |
| B | HOH7 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1 |
| Chain | Residue |
| B | ASP50 |
| B | ARG302 |
| B | HOH381 |
| B | HOH475 |
