Structure of PDB 2oym Chain B

Receptor sequence

>2oymB (length=434) Species: 1831 (Rhodococcus sp. (in: high G+C Gram-positive bacteria)) [Search protein sequence]

PSYLKDDDGRSLILRGFNTASSAKSAPDGMPQFTEADLAREYADMGTNFV
RFLISWRSVEPAPGVYDQQYLDRVEDRVGWYAERGYKVMLDMHQDVYSGA
ITPIGNGAPAWATYMDGLPVEPQPRWELYYIQPGVMRAFDNFWNTTGKHP
ELVEHYAKAWRAVADRFADNDAVVAYDLMNEPFGGSLQGPAFEAGPLAAM
YQRTTDAIRQVDQDTWVCVAPQAIGVNQGLPSGLTKIDDPRAGQQRIAYC
PHLYPLPLDHEGLARTLTDVTIDAWRANTAHTARVLGDVPIILGEFGLDT
TLPGARDYIERVYGTAREMGAGVSYWSSDPGPWGPYLPDGTQTLLVDTLN
KPYPRAVAGTPTEWSSTSDRLQLTIEPDAAITAPTEIYLPEAGFPGDVHV
EGADVVGWDRQSRLLTVRTPADSGNVTVTVTPAA

3D structure

PDB

2oym The structural basis of glycosidase inhibition by five-membered iminocyclitols: the clan a glycoside hydrolase endoglycoceramidase as a model system.

Chain

Resolution

1.86 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	MNI	B	H135 D137 W178 E179 Y182 N232 E233 F235 Y306 E351 W382	H93 D95 W126 E127 Y130 N180 E181 F183 Y254 E295 W326	MOAD: Ki=10uM

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

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:2oym, PDBe:2oym, PDBj:2oym
PDBsum	2oym
PubMed	17487923
UniProt	O33853

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