Structure of PDB 2xii Chain B

Receptor sequence
>2xiiB (length=439) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]
EIPLKYGATNEGKRQDPAMQKFRDNRLGAFIHWGLYAIPGGEWNGKVYGG
AAEWLKSWAKVPADEWLKLMDQWNPTKFDAKKWAKMAKEMGTKYVKITTK
HHEGFCLWPSKYTKYTVANTPYKRDILGELVKAYNDEGIDVHFYFSVMDW
SNPDYRYDIKSKEDSIAFSRFLEFTDNQLKELATRYPTVKDFWFDGTWDA
SVKKNGWWTAHAEQMLKELVPGVAINSRLRADDKGKRHFDSNGRLMGDYE
SGYERRLPDPVKDLKVTQWDWEACMTIPENQWGYHKDWSLSYVKTPIEVI
DRIVHAVSMGGNMVVNFGPQADGDFRPEEKAMATAIGKWMNRYGKAVYAC
DYAGFEKQDWGYYTRGKNDEVYMVVFNQPYSERLIVKTPKGITVEKATLL
TTGEDITVVETTRNEYNVSVPKKNPGEPYVIQLKVRAAK
3D structure
PDB2xii Structural and Thermodynamic Analyses of Alpha-L-Fucosidase Inhibitors.
ChainB
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.51: alpha-L-fucosidase.
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 TYR B A387 R399 D403 V405 A471 A353 R365 D369 V371 A437
BS02 TA9 B H66 E87 W88 H135 H136 Y178 D229 W232 R262 H272 E288 W316 H32 E53 W54 H101 H102 Y144 D195 W198 R228 H238 E254 W282 MOAD: Kd=63.3nM
Gene Ontology
Molecular Function
GO:0004560 alpha-L-fucosidase activity
GO:0016787 hydrolase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006004 fucose metabolic process
GO:0016139 glycoside catabolic process
Cellular Component
GO:0005764 lysosome

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Cellular Component
External links
PDB RCSB:2xii, PDBe:2xii, PDBj:2xii
PDBsum2xii
PubMed20665773
UniProtQ8A3I4

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