1TA3
Crystal Structure of xylanase (GH10) in complex with inhibitor (XIP)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0050832 | biological_process | defense response to fungus |
| B | 0000272 | biological_process | polysaccharide 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 | 0016787 | molecular_function | hydrolase activity |
| 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 SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 268 |
| Details | Domain: {"description":"GH18","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Region: {"description":"Interaction with fungal GH11 xylanase","evidences":[{"source":"PubMed","id":"15181003","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 13 |
| Details | Region: {"description":"Interaction with fungal GH10 xylanase","evidences":[{"source":"PubMed","id":"15181003","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15181003","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TE1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 281 |
| Details | Domain: {"description":"GH10","evidences":[{"source":"PROSITE-ProRule","id":"PRU01096","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| B | GLU236 | |
| B | ASP238 | |
| B | HIS206 | |
| B | GLU128 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| B | GLU128 |
