4XQ4
X-ray structure analysis of xylanase - N44D
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| 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 | 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 PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 201 |
| Chain | Residue |
| A | ASN82 |
| A | SER146 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 202 |
| Chain | Residue |
| A | SER65 |
| A | SER184 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue IOD B 201 |
| Chain | Residue |
| B | ASN82 |
| B | SER146 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue IOD B 202 |
| Chain | Residue |
| B | ASN67 |
| B | SER184 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue IOD B 203 |
| Chain | Residue |
| B | THR26 |
| B | ASN38 |
| B | HOH514 |
| B | GLY24 |
Functional Information from PROSITE/UniProt
| site_id | PS00776 |
| Number of Residues | 11 |
| Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYIVEnF |
| Chain | Residue | Details |
| A | PRO83-PHE93 |
| site_id | PS00777 |
| Number of Residues | 12 |
| Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. VavEGYFSSGsA |
| Chain | Residue | Details |
| A | VAL174-ALA185 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"26392527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"26392527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
