Structure of PDB 1y7b Chain A

Receptor sequence
>1y7bA (length=534) Species: 272562 (Clostridium acetobutylicum ATCC 824) [Search protein sequence]
SLIKNPILRGFNPDPSICRADTDYYIATSTFEWFPGVQIHHSKDLVNWHL
VAHPLNRTSLLDMKGNPNSGGIWAPDLSYHDGKFWLIYTDVKVTDGMWKD
CHNYLTTCESVDGVWSDPITLNGSGFDASLFHDNDGKKYLVNMYWDQRTY
NHNFYGIVLQEYSDKEKKLIGKAKIIYKGTDIKYTEGPHIYHIGDYYYLF
TAEGGTTYEHSETVARSKNIDGPYEIDPEYPLLTSWHDPRNSLQKCGHAS
LVHTHTDEWYLAHLVGRPLPVGNQPVLEQRGYCPLGRETSIQRIEWVDNW
PRVVGGKQGSVNVEAPKIPEVKWEKTYDEKDNFDSDKLNINFQSLRIPLT
ENIASLKAKKGNLRLYGKESLTSTFTQAFIARRWQSFKFDASTSVSFSPD
TFQQAAGLTCYYNTENWSTIQVTWNEDKGRVIDIVCCDNFHFDMPLKSNV
IPIPKDVEYIHLKVEVRVETYQYSYSFDGINWSKVPAIFESRKLSDDYVQ
GGGFFTGAFVGINCIDITGNNKPADFDYFCYKEE
3D structure
PDB1y7b Crystal structure of beta-xylosidase from Clostridium acetobutylicum
ChainA
Resolution1.6 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 CA A N333 G362 D528 N332 G361 D527
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1y7b, PDBe:1y7b, PDBj:1y7b
PDBsum1y7b
PubMed
UniProtQ97DM1

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