Structure of PDB 3c7h Chain A

Receptor sequence
>3c7hA (length=487) Species: 1423 (Bacillus subtilis) [Search protein sequence]
ATSTTIAKHIGNSNPLIDHHLGADPVALTYNGRVYIYMSSDDYEYNSNGT
IKDNSFANLNRVFVISSADMVNWTDHGAIPVAGANGANGGRGIAKWAGAS
WAPSIAVKKINGKDKFFLYFANSGGGIGVLTADSPIGPWTDPIGKPLVTP
STPGMSGVVWLFDPAVFVDDDGTGYLYAGGGVPGVSNPTQGQWANPKTAR
VIKLGPDMTSVVGSASTIDAPFMFEDSGLHKYNGTYYYSYCINFGGTHPA
DKPPGEIGYMTSSSPMGPFTYRGHFLKNPGAFFGGGGNNHHAVFNFKNEW
YVVYHAQTVSSALFGAGKGYRSPHINKLVHNADGSIQEVAANYAGVTQIS
NLNPYNRVEAETFAWNGRILTEKSTAPGGPVNNQHVTSIQNGDWIAVGNA
DFGAGGARSFKANVASTLGGKIEVRLDSADGKLVGTLNVPSTGGAQTWRE
IETAVSGATGVHKVFFVFTGTGTGNLFNFDYWQFTQR
3D structure
PDB3c7h Structural analysis of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase in complex with xylotetraose reveals a different binding mechanism compared with other members of the same family.
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
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 XYP A W101 F162 W101 F162
BS02 XYP A F224 E225 N288 F224 E225 N288
BS03 CA A E359 E361 N383 Q384 D480 E359 E361 N383 Q384 D480
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
GO:0046556 alpha-L-arabinofuranosidase activity
GO:0046872 metal ion binding
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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Cellular Component
External links
PDB RCSB:3c7h, PDBe:3c7h, PDBj:3c7h
PDBsum3c7h
PubMed18980579
UniProtQ45071|XYND_BACSU Arabinoxylan arabinofuranohydrolase (Gene Name=xynD)

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