Structure of PDB 4hk9 Chain A

Receptor sequence
>4hk9A (length=188) Species: 51453 (Trichoderma reesei) [Search protein sequence]
IQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGHFVGGKGWQ
PGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPSTGA
TKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSVNT
ANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS
3D structure
PDB4hk9 X-ray crystallographic studies of family 11 xylanase Michaelis and product complexes: implications for the catalytic mechanism.
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H44 Y77 E86 Y88 E177
Catalytic site (residue number reindexed from 1) H42 Y75 E84 Y86 E175
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 H44 V46 Y77 E86 Y88 R122 P126 E177 H42 V44 Y75 E84 Y86 R120 P124 E175
BS02 XYP A W18 Y77 P126 S127 Y171 W16 Y75 P124 S125 Y169
BS03 XYP A S127 I128 S125 I126
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:4hk9, PDBe:4hk9, PDBj:4hk9
PDBsum4hk9
PubMed24419374
UniProtP36217|XYN2_HYPJR Endo-1,4-beta-xylanase 2 (Gene Name=xyn2)

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