Structure of PDB 3fef Chain C

Receptor sequence
>3fefC (length=434) Species: 1423 (Bacillus subtilis) [Search protein sequence]
LDQIKIAYIGGGSQGWARSLMSDLSIDERMSGTVALYDLDFEAAQKNEVI
GNHSGNGRWRYEAVSTLKKALSAADIVIISILPGSLDDMEVDVHLPERCG
IYQSVGDTVGPGGIIRGLRAVPIFAEIARAIRDYAPESWVINYTNPMSVC
TRVLYKVFPGIKAIGCCHEVFGTQKLLAEMVTERLGIEVPRREDIRVNVL
GINHFTWITKASYRHIDLLPIFREFSAHYGESGYELEGECWRDSVFCSAH
RVAFDLFETYGAIPAAGDRHLAEFLPGPYLKQPEVWKFHLTPISFRKQDR
AEKRQETERLIVQQRGVAEKASGEEGVNIIAALLGLGELVTNVNMPNQGQ
VLNLPIQAIVETNAFITRNRVQPILSGALPKGVEMLAARHISNQEAVADA
GLTKDTGLAFQAFLNDPLVQIDRSDAEQLFNDML
3D structure
PDB3fef Crystal structure of putative glucosidase lplD from bacillus subtilis.
ChainC
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.67: galacturonan 1,4-alpha-galacturonidase.
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 MG C C173 H210 C167 H204
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
GO:0047911 galacturan 1,4-alpha-galacturonidase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3fef, PDBe:3fef, PDBj:3fef
PDBsum3fef
PubMed
UniProtP39130|LPLD_BACSU Alpha-galacturonidase (Gene Name=lplD)

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