Structure of PDB 1qh6 Chain B

Receptor sequence
>1qh6B (length=207) Species: 76935 (Salipaludibacillus agaradhaerens) [Search protein sequence]
QIVTDNSIGNHDGYDYEFWKDSGGSGTMILNHGGTFSAQWNNVNNILFRK
GKKFNETQTHQQVGNMSINYGANFQPNGNAYLCVYGWTVDPLVEYYIVDS
WGNWRPPGATPKGTITVDGGTYDIYETLRVNQPSIKGIATFKQYWSVRRS
KRTSGTISVSNHFRAWENLGMNMGKMYEVALTVEGYQSSGSANVYSNTLR
INGNPLS
3D structure
PDB1qh6 Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N45 Y85 E94 Y96 E184
Catalytic site (residue number reindexed from 1) N45 Y85 E94 Y96 E184
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 X2F B Y85 E94 R129 P133 F141 Y85 E94 R129 P133 F141
BS02 XYP B E17 W19 R49 Y85 P133 S134 E17 W19 R49 Y85 P133 S134
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:1qh6, PDBe:1qh6, PDBj:1qh6
PDBsum1qh6
PubMed10381409
UniProtQ7SIE3

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