Structure of PDB 1qw8 Chain A

Receptor sequence
>1qw8A (length=497) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
KATMIIEKDFKIAEIDKRIYGSFIEHLGRAVYGGIYEPGHPQADENGFRQ
DVIELVKELQVPIIRYPGGNFVSGYNWEDGVGPKEQRPRRLDLAWKSVET
NEIGLNEFMDWAKMVGAEVNMAVNLGTRGIDAARNLVEYCNHPSGSYYSD
LRIAHGYKEPHKIKTWCLGNAMDGPWQIGHKTAVEYGRIACEAAKVMKWV
DPTIELVVCGSSNRNMPTFAEWEATVLDHTYDHVDYISLHQYYGNRDNDT
ANYLALSLEMDDFIRSVVAIADYVKAKKRSKKTIHLSFDEWNVWYHSNEA
DKLIEPWTVAPPLLEDIYNFEDALLVGCMLITLMKHADRVKIACLAQLVN
VIAPIMTEKNGPAWKQTIYYPFMHASVYGRGVALHPVISSPKYDSKDFTD
VPYLESIAVYNEEKEEVTIFAVNRDMEDALLLECDVRSFEDYRVIEHIVL
EHDNVKQTNSAQSSPVVPHRNGDAQLSDRKVSATLPKLSWNVIRLGK
3D structure
PDB1qw8 Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A175 E294
Catalytic site (residue number reindexed from 1) A171 E290
Enzyme Commision number 3.2.1.55: non-reducing end alpha-L-arabinofuranosidase.
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 AHR A E29 G73 N74 N174 Y246 E294 Q351 E25 G69 N70 N170 Y242 E290 Q347
Gene Ontology
Molecular Function
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046556 alpha-L-arabinofuranosidase activity
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0031222 arabinan catabolic process
GO:0046373 L-arabinose metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qw8, PDBe:1qw8, PDBj:1qw8
PDBsum1qw8
PubMed14517232
UniProtQ9XBQ3|IABF_GEOSE Intracellular exo-alpha-(1->5)-L-arabinofuranosidase (Gene Name=abfA)

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