2D1Z
Crystal structure of catalytic-site mutant xylanase from Streptomyces olivaceoviridis E-86
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 | 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 | 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 | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1441 |
Chain | Residue |
B | SER631 |
B | ARG639 |
B | ASP640 |
B | HOH2005 |
B | HOH2094 |
B | HOH2299 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 1442 |
Chain | Residue |
A | ASP140 |
A | SER131 |
A | ASP132 |
A | ARG139 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 1443 |
Chain | Residue |
A | TYR172 |
A | ASN173 |
A | HIS207 |
A | ASN209 |
A | ARG275 |
A | HOH1571 |
A | HOH1820 |
A | HOH1847 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 1444 |
Chain | Residue |
A | GLU357 |
A | ARG359 |
A | TRP383 |
A | GLY384 |
A | HOH1528 |
A | HOH1676 |
A | HOH1709 |
B | ALA855 |
B | GLU857 |
B | GLY884 |
B | LYS889 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 1445 |
Chain | Residue |
A | ASP408 |
A | ALA409 |
A | GLY411 |
A | GLY412 |
A | GLN421 |
A | TYR423 |
A | ASN430 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 1446 |
Chain | Residue |
A | ASP325 |
A | VAL326 |
A | PRO327 |
A | ASN328 |
A | GLN338 |
A | TYR340 |
A | HIS343 |
A | ASN347 |
A | HOH1660 |
A | HOH1870 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 1941 |
Chain | Residue |
B | SER597 |
B | ARG645 |
B | HOH1986 |
B | HOH2206 |
B | HOH2233 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 1942 |
Chain | Residue |
B | LYS548 |
B | TRP585 |
B | GLN588 |
B | HIS628 |
B | HOH2109 |
B | HOH2391 |
B | HOH2394 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 1943 |
Chain | Residue |
B | LYS524 |
B | THR771 |
B | ASP772 |
B | SER773 |
B | HOH1978 |
B | HOH2097 |
B | HOH2189 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 1944 |
Chain | Residue |
B | TYR672 |
B | ASN673 |
B | HIS707 |
B | ASN709 |
B | ARG775 |
B | HOH2109 |
B | HOH2261 |
B | HOH2418 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 1945 |
Chain | Residue |
B | ASP825 |
B | ASN828 |
B | TYR840 |
B | HIS843 |
B | ASN847 |
B | HOH2369 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 1946 |
Chain | Residue |
B | ASP908 |
B | ALA909 |
B | VAL910 |
B | GLY911 |
B | GLY912 |
B | GLN921 |
B | TYR923 |
B | ASN930 |
Functional Information from PROSITE/UniProt
site_id | PS00591 |
Number of Residues | 11 |
Details | GH10_1 Glycosyl hydrolases family 10 (GH10) active site. GVDVaITELDI |
Chain | Residue | Details |
A | GLY229-ILE239 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2his |
Chain | Residue | Details |
A | HIS128 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2his |
Chain | Residue | Details |
B | HIS628 |