4HK8
Crystal Structures of Mutant Endo- -1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)
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 | 0008152 | biological_process | 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 |
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374 |
Chain | Residue | Details |
A | TYR87 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374 |
Chain | Residue | Details |
A | GLY178 |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24419374 |
Chain | Residue | Details |
A | LEU74 | |
A | GLY78 | |
A | ILE89 | |
A | VAL123 | |
A | SER127 | |
A | TYR137 | |
A | GLN172 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:16790934 |
Chain | Residue | Details |
A | THR2 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | TRP39 | |
A | PHE62 |