Structure of PDB 2qz2 Chain A

Receptor sequence
>2qz2A (length=183) Species: 5061 (Aspergillus niger) [Search protein sequence]
SAGINYVQNYNGNLGDFTYDESAGTFSMYWEDGVSSDFVVGLGWTTGSSN
AITYSAEYSASGSSSYLAVYGWVNYPQAEYYIVEDYGDYNPCSSATSLGT
VYSDGSTYQVCTDTRTNEPSITGTSTFTQYFSVRESTRTSGTVTVANHFN
FWAQHGFGNSDFNYQVVAVAAWSGAGSASVTIS
3D structure
PDB2qz2 Crystallographic analysis shows substrate binding at the -3 to +1 active-site subsites and at the surface of glycoside hydrolase family 11 endo-1,4-beta-xylanases.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D37 Y70 E79 Y81 A170
Catalytic site (residue number reindexed from 1) D37 Y70 E79 Y81 A170
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 D37 E79 P119 D37 E79 P119
BS02 XYP A Y10 Y70 P119 S120 Y164 Y10 Y70 P119 S120 Y164
BS03 XYP A N13 L14 G15 N13 L14 G15
BS04 XYP A Y29 W30 E31 D32 Y29 W30 E31 D32
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:2qz2, PDBe:2qz2, PDBj:2qz2
PDBsum2qz2
PubMed17983355
UniProtP55329|XYNA_ASPNG Endo-1,4-beta-xylanase A (Gene Name=xynA)

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