Structure of PDB 1h4g Chain A

Receptor sequence
>1h4gA (length=206) Species: 76935 (Salipaludibacillus agaradhaerens) [Search protein sequence]
EIVTDNSIGNHDGYDYEFWKDSGGSGTMILNHGGTFSAQWNNVNNILFRK
GKKFNETQTHQQVGNMSINYGANFQPNGNAYLCVYGWTVDPLVEYYIVDS
WGNWRPPGATPKGTITVDGGTYDIYETLRVNQPSIKGIATFKQYWSVRRS
KRTSGTISVSNHFRAWENLGMNMGKMYEVALTVEGYQSSGSANVYSNTLR
INGNPL
3D structure
PDB1h4g 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.
ChainA
Resolution1.1 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 A L47 Y85 E94 R129 P133 F141 L47 Y85 E94 R129 P133 F141
BS02 XYP A E17 W19 R49 Y85 S134 E17 W19 R49 Y85 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:1h4g, PDBe:1h4g, PDBj:1h4g
PDBsum1h4g
PubMed10381409
UniProtQ7SIE3

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