Structure of PDB 5zii Chain A

Receptor sequence
>5ziiA (length=189) Species: 1344414 (Trichoderma reesei RUT C-30) [Search protein sequence]
TIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGNFVGGKGW
QPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYFIVENFGTYNPSTG
ATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSVN
TANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS
3D structure
PDB5zii Direct determination of protonation states and visualization of hydrogen bonding in a glycoside hydrolase with neutron crystallography.
ChainA
Resolution1.3 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 F88 E177
Catalytic site (residue number reindexed from 1) N43 Y76 E85 F87 E176
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 W18 V46 E86 R122 P126 E177 W17 V45 E85 R121 P125 E176
BS02 XYP A W18 Y77 S127 Y171 W17 Y76 S126 Y170
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:5zii, PDBe:5zii, PDBj:5zii
PDBsum5zii
PubMed
UniProtP36217|XYN2_HYPJR Endo-1,4-beta-xylanase 2 (Gene Name=xyn2)

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