Structure of PDB 3c7f Chain A

Receptor sequence

>3c7fA (length=487) Species: 1423 (Bacillus subtilis)

ATSTTIAKHIGNSNPLIDHHLGADPVALTYNGRVYIYMSSDDYEYNSNGT
IKDNSFANLNRVFVISSADMVNWTDHGAIPVAGANGANGGRGIAKWAGAS
WAPSIAVKKINGKDKFFLYFANSGGGIGVLTADSPIGPWTDPIGKPLVTP
STPGMSGVVWLFDPAVFVDDDGTGYLYAGGGVPGVSNPTQGQWANPKTAR
VIKLGPDMTSVVGSASTIDAPFMFEDSGLHKYNGTYYYSYCINFGGTHPA
DKPPGEIGYMTSSSPMGPFTYRGHFLKNPGAFFGGGGNNHHAVFNFKNEW
YVVYHAQTVSSALFGAGKGYRSPHINKLVHNADGSIQEVAANYAGVTQIS
NLNPYNRVEAETFAWNGRILTEKSTAPGGPVNNQHVTSIQNGDWIAVGNA
DFGAGGARSFKANVASTLGGKIEVRLDSADGKLVGTLNVPSTGGAQTWRE
IETAVSGATGVHKVFFVFTGTGTGNLFNFDYWQFTQR

3D structure

• PDB: 3c7f 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.
• Chain: A
• Resolution: 1.55 Å

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	F224 F244	F224 F244
BS02	XYP	A	E225 N288	E225 N288
BS03	XYP	A	W101 W160 F162	W101 W160 F162
BS04	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

External links

• PDB: RCSB:3c7f, PDBe:3c7f, PDBj:3c7f
• PDBsum: 3c7f
• PubMed: 18980579
• UniProt: Q45071|XYND_BACSU Arabinoxylan arabinofuranohydrolase (Gene Name=xynD)