Structure of PDB 1bcx Chain A Binding Site BS01
Receptor Information
>1bcx Chain A (length=185) Species:
1397
(Niallia circulans) [
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ASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGNFVVGKGWTTGSPFRT
INYNAGVWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTYKGTVKS
DGGTYDIYTTTRYNAPSIDGDRTTFTQYWSVRQSKRPTGSNATITFTNHV
NAWKSHGMNLGSNWAYQVMATCGYQSSGSSNVTVW
Ligand information
Ligand ID
XYP
InChI
InChI=1S/C5H10O5/c6-2-1-10-5(9)4(8)3(2)7/h2-9H,1H2/t2-,3+,4-,5-/m1/s1
InChIKey
SRBFZHDQGSBBOR-KKQCNMDGSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
C1C(C(C(C(O1)O)O)O)O
CACTVS 3.341
O[C@@H]1CO[C@@H](O)[C@H](O)[C@H]1O
OpenEye OEToolkits 1.5.0
C1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O
CACTVS 3.341
O[CH]1CO[CH](O)[CH](O)[CH]1O
ACDLabs 10.04
OC1C(O)COC(O)C1O
Formula
C5 H10 O5
Name
beta-D-xylopyranose;
beta-D-xylose;
D-xylose;
xylose
ChEMBL
DrugBank
ZINC
ZINC000001529215
PDB chain
1bcx Chain B Residue 1 [
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Receptor-Ligand Complex Structure
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PDB
1bcx
Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase.
Resolution
1.81 Å
Binding residue
(original residue number in PDB)
V37 E78 R112 P116
Binding residue
(residue number reindexed from 1)
V37 E78 R112 P116
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
N35 Y69 E78 Y80 C172
Catalytic site (residue number reindexed from 1)
N35 Y69 E78 Y80 C172
Enzyme Commision number
3.2.1.8
: endo-1,4-beta-xylanase.
Gene Ontology
Molecular Function
GO:0004553
hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798
hydrolase activity, acting on glycosyl bonds
GO:0031176
endo-1,4-beta-xylanase activity
Biological Process
GO:0005975
carbohydrate metabolic process
GO:0045493
xylan catabolic process
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:1bcx
,
PDBe:1bcx
,
PDBj:1bcx
PDBsum
1bcx
PubMed
8019418
UniProt
P09850
|XYNA_NIACI Endo-1,4-beta-xylanase (Gene Name=xlnA)
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