Structure of PDB 2dfb Chain A

Receptor sequence
>2dfbA (length=190) Species: 51453 (Trichoderma reesei) [Search protein sequence]
QTIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGNFVGGKG
WQPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPST
GATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSV
NTANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS
3D structure
PDB2dfb Structure of an orthorhombic form of xylanase II from Trichoderma reesei and analysis of thermal displacement.
ChainA
Resolution1.11 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N44 Y77 E86 Y88 E177
Catalytic site (residue number reindexed from 1) N44 Y77 E86 Y88 E177
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 IOD A P68 G94 P68 G94
BS02 IOD A S65 S184 A185 S65 S184 A185
BS03 IOD A G30 Q34 S36 G30 Q34 S36
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
Cellular Component
GO:0005576 extracellular region

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Cellular Component
External links
PDB RCSB:2dfb, PDBe:2dfb, PDBj:2dfb
PDBsum2dfb
PubMed16790934
UniProtP36217|XYN2_HYPJR Endo-1,4-beta-xylanase 2 (Gene Name=xyn2)

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