3M4F
Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum
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 |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CXS A 206 |
| Chain | Residue |
| A | TYR35 |
| A | TYR93 |
| A | ARG138 |
| A | HOH459 |
| A | HOH473 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CXS A 207 |
| Chain | Residue |
| A | HOH227 |
| A | HOH252 |
| A | HOH313 |
| A | HOH572 |
| B | THR167 |
| B | GLY169 |
| B | ASN170 |
| B | ASN173 |
| A | SER126 |
| A | ASP127 |
| A | ASN170 |
| A | HOH210 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CXS B 206 |
| Chain | Residue |
| B | TYR35 |
| B | TYR93 |
| B | ARG138 |
| B | PRO142 |
| B | HOH309 |
| B | HOH615 |
| B | HOH714 |
| C | HOH496 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CXS C 206 |
| Chain | Residue |
| C | TYR35 |
| C | TYR93 |
| C | PRO142 |
| C | HOH546 |
| C | HOH555 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CXS D 206 |
| Chain | Residue |
| D | GLN33 |
| D | TYR35 |
| D | TYR93 |
| D | PRO142 |
| D | HOH387 |
| D | HOH435 |
Functional Information from PROSITE/UniProt
| site_id | PS00776 |
| Number of Residues | 11 |
| Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PQaEYYIVEsY |
| Chain | Residue | Details |
| A | PRO99-TYR109 |
