Structure of PDB 1bcx Chain A

Receptor sequence
>1bcxA (length=185) Species: 1397 (Niallia circulans) [Search protein sequence]
ASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGNFVVGKGWTTGSPFRT
INYNAGVWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTYKGTVKS
DGGTYDIYTTTRYNAPSIDGDRTTFTQYWSVRQSKRPTGSNATITFTNHV
NAWKSHGMNLGSNWAYQVMATCGYQSSGSSNVTVW
3D structure
PDB1bcx Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase.
ChainA
Resolution1.81 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 XYP A V37 E78 R112 P116 V37 E78 R112 P116
BS02 XYP A Q7 W9 Y69 P116 S117 Y166 Q7 W9 Y69 P116 S117 Y166
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1bcx, PDBe:1bcx, PDBj:1bcx
PDBsum1bcx
PubMed8019418
UniProtP09850|XYNA_NIACI Endo-1,4-beta-xylanase (Gene Name=xlnA)

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