4XUY
Crystal structure of an endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10) enzyme from Aspergillus niger
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005576 | cellular_component | extracellular region |
| 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 |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005576 | cellular_component | extracellular region |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 401 |
| Chain | Residue |
| A | SER88 |
| A | SER90 |
| A | GLY91 |
| A | HOH555 |
| A | HOH615 |
| A | HOH721 |
| B | THR33 |
| B | GLN86 |
| B | HOH523 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | SER164 |
| A | LEU165 |
| A | HIS216 |
| A | HOH533 |
| B | LYS127 |
| B | HOH550 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | TYR50 |
| A | THR51 |
| A | GLU72 |
| A | ASP299 |
| A | HOH526 |
| A | HOH567 |
| B | ASN103 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| A | THR33 |
| A | GLN86 |
| B | SER88 |
| B | SER90 |
| B | GLY91 |
| B | HOH507 |
| B | HOH549 |
| B | HOH629 |
| B | HOH752 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| A | ARG302 |
| A | SER305 |
| B | SER215 |
| B | HOH525 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| A | ASN103 |
| B | TYR50 |
| B | THR51 |
| B | GLU72 |
| B | ASP299 |
| B | HOH782 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 404 |
| Chain | Residue |
| B | SER164 |
| B | LEU165 |
| B | HIS216 |
| B | HOH553 |
Functional Information from PROSITE/UniProt
| site_id | PS00591 |
| Number of Residues | 11 |
| Details | GH10_1 Glycosyl hydrolases family 10 (GH10) active site. TKEIaVTELDI |
| Chain | Residue | Details |
| A | THR256-ILE266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU157 | |
| B | GLU157 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10061 |
| Chain | Residue | Details |
| A | GLU263 | |
| B | GLU263 |
