Structure of PDB 2oyl Chain A

Receptor sequence
>2oylA (length=434) Species: 1831 (Rhodococcus sp. (in: high G+C Gram-positive bacteria)) [Search protein sequence]
PSYLKDDDGRSLILRGFNTASSAKSAPDGMPQFTEADLAREYADMGTNFV
RFLISWRSVEPAPGVYDQQYLDRVEDRVGWYAERGYKVMLDMHQDVYSGA
ITPAIGNGAPAWATYMDGLPVEPQPRWELYYIQPGVMRAFDNFWNTTGKH
PELVEHYAKAWRAVADRFADNDAVVAYDLMNEPFGGSLQGPAFEAGPLAA
MYQRTTDAIRQVDQDTWVCVAPQAIGVNQGLPSGLTKIDDPRAGQQRIAY
CPHLYPLPLHEGLARTLTDVTIDAWRANTAHTARVLGDVPIILGEFGLDT
TLPGARDYIERVYGTAREMGAGVSYWSSDPGPWGPYLPDGTQTLLVDTLN
KPYPRAVAGTPTEWSSTSDRLQLTIEPDAAITAPTEIYLPEAGFPGDVHV
EGADVVGWDRQSRLLTVRTPADSGNVTVTVTPAA
3D structure
PDB2oyl The structural basis of glycosidase inhibition by five-membered iminocyclitols: the clan a glycoside hydrolase endoglycoceramidase as a model system.
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.123: endoglycosylceramidase.
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 IDC A K66 H135 D137 W178 N232 E233 Y306 E351 W382 K24 H93 D95 W127 N181 E182 Y255 E295 W326 MOAD: Ki=0.5uM
PDBbind-CN: -logKd/Ki=6.30,Ki=0.5uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0047876 endoglycosylceramidase activity
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
GO:0016042 lipid catabolic process
GO:1901136 carbohydrate derivative catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2oyl, PDBe:2oyl, PDBj:2oyl
PDBsum2oyl
PubMed17487923
UniProtO33853

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