Structure of PDB 7dfo Chain F

Receptor sequence
>7dfoF (length=194) Species: 1921 (Streptomyces olivaceoviridis) [Search protein sequence]
ATVITTNQTGTNNGFYYSFWTDGGGSVSMTLNSGGNYSTSWTNCGNFVAG
KGWSNGGRRNVQYSGSFYPSGNGYLALYGWTSNPLVEYYIVDNWGNYRPT
GTYKGTVTSDGGTYDVYQTTRYNAPSVEGTKTFNQYWSVRQSKRTGGTIT
TGNHFDAWARYGMQLGSFSYYMILATEGYQSSGSSNLTVSGKLA
3D structure
PDB7dfo Structure-based substrate specificity analysis of GH11 xylanase from Streptomyces olivaceoviridis E-86.
ChainF
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N46 Y78 E87 Y89 E177
Catalytic site (residue number reindexed from 1) N46 Y78 E87 Y89 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 XYP F W20 N46 V48 E87 R121 P125 E177 W20 N46 V48 E87 R121 P125 E177
BS02 XYP F W20 Y78 S126 Y171 W20 Y78 S126 Y171
BS03 GCV F N7 W20 N7 W20
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7dfo, PDBe:7dfo, PDBj:7dfo
PDBsum7dfo
PubMed33564921
UniProtA0A7G1MBT0

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