1TE1
Crystal structure of family 11 xylanase in complex with inhibitor (XIP-I)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004568 | molecular_function | chitinase activity |
A | 0004857 | molecular_function | enzyme inhibitor activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006952 | biological_process | defense response |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0050832 | biological_process | defense response to fungus |
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 PROSITE/UniProt
site_id | PS00776 |
Number of Residues | 11 |
Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLvEYYILEsY |
Chain | Residue | Details |
B | PRO82-TYR92 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062 |
Chain | Residue | Details |
B | GLU85 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
B | GLU176 | |
A | ASN265 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | SITE: Interaction with protein inhibitor XIP-I => ECO:0000269|PubMed:15181003 |
Chain | Residue | Details |
B | ASN10 | |
B | TYR136 | |
B | GLU142 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bvv |
Chain | Residue | Details |
B | GLU85 | |
B | GLU176 |