Structure of PDB 2qz3 Chain A

Receptor sequence
>2qz3A (length=184) Species: 1423 (Bacillus subtilis) [Search protein sequence]
STDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGNFVVGKGWTTGSPFRTI
NYNAGVWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTYKGTVKSD
GGTYDIYTTTRYNAPSIDGDRTTFTQYWSVRQSKRPTGSNATITFSNHVN
AWKSHGMNLGSNWAYQVMATAGYQSSGSSNVTVW
3D structure
PDB2qz3 Crystallographic analysis shows substrate binding at the -3 to +1 active-site subsites and at the surface of glycoside hydrolase family 11 endo-1,4-beta-xylanases.
ChainA
Resolution1.8 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 A172
Catalytic site (residue number reindexed from 1) N34 Y68 E77 Y79 A171
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 W9 V37 Y69 E78 R112 P116 W8 V36 Y68 E77 R111 P115
BS02 XYP A W9 Y69 P116 S117 Y166 W8 Y68 P115 S116 Y165
BS03 XYP A N54 G56 N181 T183 N53 G55 N180 T182
BS04 XYP A N141 W185 N140 W184
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:2qz3, PDBe:2qz3, PDBj:2qz3
PDBsum2qz3
PubMed17983355
UniProtP18429|XYNA_BACSU Endo-1,4-beta-xylanase A (Gene Name=xynA)

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