2B42
Crystal structure of the Triticum xylanse inhibitor-I in complex with bacillus subtilis xylanase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0045493 | biological_process | xylan catabolic process |
| 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 |
Functional Information from PROSITE/UniProt
| site_id | PS00776 |
| Number of Residues | 11 |
| Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW |
| Chain | Residue | Details |
| B | PRO75-TRP85 |
| site_id | PS00777 |
| Number of Residues | 12 |
| Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS |
| Chain | Residue | Details |
| B | MET169-SER180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:7911679 |
| Chain | Residue | Details |
| B | GLU78 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063 |
| Chain | Residue | Details |
| B | GLU172 |
