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Structure of PDB 3vsu Chain D

Receptor sequence
>3vsuD (length=638) [Search protein sequence]
MEYHVAKTGSDEGKGTLKDPFLTINKAASVAMAGDTIIVHEGVYREWVKP
KYKGLSDKRRITYKAAEGEKVVIKGSERIQSWQRVEGNVWRCQLPNSFFG
EFNPYKEEVFGDWLLTVNEKKHLGDVYLNGMSFYEVTNYEDLFNPQLRTE
VLDHWTQKIVPIKNAEQTKYVWYAEVDREKTTIYANFQGADPNEEFVEIN
VRRSCFYPVETGIDYITVKGFEMAHAATPWAPPTADQPGLIGPNWSKGWI
IEDNIIHDAKCSAISIGKEATTGNNYRSIRKDKPGYQYQLEAVFNAKRNG
WSKEKIGSHIIRNNTIYDCGQNAIVGHLGGVFSEIYNNHIYNIALKREFY
GHEIAGIKLHAAIDVQIHHNRIHDCSLGLWLDWEAQGTRVSKNLFYNNNR
DVFVEVSHGPYLVDHNILSSEYAIDNMSQGGAYINNLIAGKMNQRKVLNR
STQYHLPHSTEVAGFAFVYGGDDRFYNNIFIGKEGLENVGTSHYNNCTTS
LEEYIEKVNEVPGDLGEFERVEQPVYINKNAYFNGAEPFEKEKDNLVKKD
FDPKLAIIDEGDEVYLSLQLPDEFENIVGDIHSTKTLERVRIVDAEYESP
DGKELVLDTDYLDAKKPENSSIGPIALLKKGNNYIKVW
3D structure
PDB3vsu The substrate/product-binding modes of a novel GH120 beta-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485
ChainD
Resolution2.05 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.37: xylan 1,4-beta-xylosidase.
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 D W155 H352 F403 E405 R450 W155 H352 F403 E405 R450
BS02 XYP D W113 P233 Q289 H352 E353 K358 H360 W380 D382 W383 E405 R450 W113 P233 Q289 H352 E353 K358 H360 W380 D382 W383 E405 R450
Gene Ontology
Molecular Function
GO:0016837 carbon-oxygen lyase activity, acting on polysaccharides
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links

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