Structure of PDB 3lgr Chain A

Receptor sequence
>3lgrA (length=190) Species: 51453 (Trichoderma reesei) [Search protein sequence]
QTIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGNFVGGKG
WQPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPST
GATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSV
NTANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS
3D structure
PDB3lgr A dipicolinate lanthanide complex for solving protein structures using anomalous diffraction.
ChainA
Resolution1.64 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 PDC A Q4 P5 N19 G21 G23 Q4 P5 N19 G21 G23
BS02 PDC A Q4 Y17 Q4 Y17
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:3lgr, PDBe:3lgr, PDBj:3lgr
PDBsum3lgr
PubMed20606256
UniProtP36217|XYN2_HYPJR Endo-1,4-beta-xylanase 2 (Gene Name=xyn2)

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