3KL0
Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004348 | molecular_function | glucosylceramidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006665 | biological_process | sphingolipid metabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0033940 | molecular_function | glucuronoarabinoxylan endo-1,4-beta-xylanase activity |
A | 0045493 | biological_process | xylan catabolic process |
B | 0004348 | molecular_function | glucosylceramidase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0006665 | biological_process | sphingolipid metabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0033940 | molecular_function | glucuronoarabinoxylan endo-1,4-beta-xylanase activity |
B | 0045493 | biological_process | xylan catabolic process |
C | 0004348 | molecular_function | glucosylceramidase activity |
C | 0005576 | cellular_component | extracellular region |
C | 0006665 | biological_process | sphingolipid metabolic process |
C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
C | 0033940 | molecular_function | glucuronoarabinoxylan endo-1,4-beta-xylanase activity |
C | 0045493 | biological_process | xylan catabolic process |
D | 0004348 | molecular_function | glucosylceramidase activity |
D | 0005576 | cellular_component | extracellular region |
D | 0006665 | biological_process | sphingolipid metabolic process |
D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
D | 0033940 | molecular_function | glucuronoarabinoxylan endo-1,4-beta-xylanase activity |
D | 0045493 | biological_process | xylan catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MLA A 402 |
Chain | Residue |
A | TRP268 |
A | TYR269 |
A | ARG272 |
A | TYR274 |
A | HIS405 |
A | HIS406 |
A | HOH614 |
A | HOH840 |
A | HOH1759 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MLA A 403 |
Chain | Residue |
A | ARG353 |
A | THR366 |
A | HIS378 |
A | HOH446 |
A | HOH728 |
A | HOH753 |
C | ASN338 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TAR A 404 |
Chain | Residue |
A | LYS13 |
A | ARG303 |
A | ASP305 |
A | ALA306 |
A | HOH416 |
A | HOH591 |
A | HOH1072 |
B | LYS126 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE HIS A 405 |
Chain | Residue |
A | GLU140 |
A | TYR143 |
A | TYR204 |
A | TYR231 |
A | MLA402 |
A | HIS406 |
A | HOH840 |
A | HOH1544 |
A | HOH1648 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE HIS A 406 |
Chain | Residue |
A | TYR204 |
A | GLU229 |
A | TRP268 |
A | MLA402 |
A | HIS405 |
A | HOH1527 |
A | HOH1544 |
A | HOH1859 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 407 |
Chain | Residue |
A | HOH490 |
A | HOH541 |
A | HOH556 |
A | HOH950 |
A | HOH952 |
C | HOH481 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MLA B 402 |
Chain | Residue |
A | HIS398 |
B | TRP268 |
B | TYR269 |
B | ARG272 |
B | TYR274 |
B | HOH423 |
B | HOH477 |
B | HOH1740 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 403 |
Chain | Residue |
A | HOH552 |
B | HOH426 |
B | HOH484 |
B | HOH563 |
B | HOH955 |
B | HOH2148 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MLA C 402 |
Chain | Residue |
B | HIS395 |
B | HIS396 |
C | TRP268 |
C | TYR269 |
C | ARG272 |
C | TYR274 |
C | HOH1359 |
C | HOH1371 |
C | HOH1693 |
D | HOH494 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA C 403 |
Chain | Residue |
C | HOH424 |
C | HOH457 |
C | HOH1099 |
C | HOH1111 |
C | HOH2157 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MLA D 402 |
Chain | Residue |
C | HOH2086 |
D | TRP268 |
D | TYR269 |
D | ARG272 |
D | TYR274 |
D | HOH435 |
D | HOH1756 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA D 403 |
Chain | Residue |
D | HOH432 |
D | HOH499 |
D | HOH834 |
D | HOH880 |
D | HOH887 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:21256135 |
Chain | Residue | Details |
A | GLU140 | |
B | GLU140 | |
C | GLU140 | |
D | GLU140 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:21256135 |
Chain | Residue | Details |
A | GLU229 | |
B | GLU229 | |
C | GLU229 | |
D | GLU229 |