Structure of PDB 4hkw Chain A

Receptor sequence
>4hkwA (length=190) Species: 51453 (Trichoderma reesei) [Search protein sequence]
QTIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGNFVGGKG
WQPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPST
GATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSV
NTANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS
3D structure
PDB4hkw X-ray crystallographic studies of family 11 xylanase Michaelis and product complexes: implications for the catalytic mechanism.
ChainA
Resolution1.65 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 XYS A N71 Y96 N71 Y96
BS02 XYP A N71 Y96 Y179 N71 Y96 Y179
BS03 XYP A Y73 Y88 R122 W138 E177 Y73 Y88 R122 W138 E177
BS04 XYP A W18 Y77 S127 Y171 W18 Y77 S127 Y171
BS05 XYP A S127 I128 S127 I128
BS06 CA A N92 F93 H144 N92 F93 H144
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4hkw, PDBe:4hkw, PDBj:4hkw
PDBsum4hkw
PubMed24419374
UniProtP36217|XYN2_HYPJR Endo-1,4-beta-xylanase 2 (Gene Name=xyn2)

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