Structure of PDB 2wsp Chain A

Receptor sequence
>2wspA (length=435) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
KPRYKPDWESLREHTVPKWFDKAKFGIFIHWGIYSVPGWATPTGELGVPM
DAWFFQNPYAEWYENSLRIKESPTWEYHVKTYGENFEYEKFADLFTAEKW
DPQEWADLFKKAGAKYVIPTTKHHDGFCLWGTKYTDFNSVKRGPKRDLVG
DLAKAVREAGLRFGVYYSGGLDWRFTTEPIRYPEDLSYIRPNTYEYADYA
YKQVMELVDLYLPDVLWNGMGWPEKGKEDLKYLFAYYYNKHPEGSVNDRW
GVPHWDFKTAEYLPGYKWEFTRGIGLSFGYNRNEGPEHMLSVEQLVYTLV
DVVSKGGNLLLNVGPKGDGTIPDLQKERLLGLGEWLRKYGDAIYGTSVWE
RCCAKTEDGTEIRFTRKCNRIFVIFLGIPTGEKIVIEDLNLSAGTVRHFL
TGERLSFKNVGKNLEITVPKKLLETDSITLVLEAV
3D structure
PDB2wsp Beta-Glycosyl Azides as Substrates for Alpha-Glycosynthases: Preparation of Novel Efficient Alpha-L-Fucosynthases
ChainA
Resolution2.65 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 FUY A Y64 W67 E266 Y59 W62 E261
BS02 FUC A H34 E66 W67 H128 H129 F290 H30 E61 W62 H123 H124 F278
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2wsp, PDBe:2wsp, PDBj:2wsp
PDBsum2wsp
PubMed19875083
UniProtQ9WYE2

[Back to BioLiP]