Structure of PDB 1odu Chain A

Receptor sequence
>1oduA (length=422) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
RYKPDWESLREHTVPKWFDKAKFGIFIHWGIYSVPGWATPDAWFFQNPYA
EWYENSLRIKESPTWEYHVKTYGENFEYEKFADLFTAEKWDPQEWADLFK
KAGAKYVIPTTKHHDGFCLWGTKYTDFNSVKRGPKRDLVGDLAKAVREAG
LRFGVYYSGGLDWRFTTEPIRYPEDLSYIRPNTYEYADYAYKQVMELVDL
YLPDVLWNDMGWPEKGKEDLKYLFAYYYNKHPEGSVNDRWGVPHWDFKTA
EDLPGYKWEFTRGIGLSFGYNRNEHMLSVEQLVYTLVDVVSKGGNLLLNV
GPKGDGTIPDLQKERLLGLGEWLRKYGDAIYGTSVWERCCAKTEDGTEIR
FTRKCNRIFVIFLGIPTGEKIVIEDLNLSAGTVRHFLTGERLSFKNVGKN
LEITVPKKLLETDSITLVLEAV
3D structure
PDB1odu Crystal Structure of Thermotoga Maritima {Alpha}-L-Fucosidase: Insights Into the Catalytic Mechanism and the Molecular Basis for Fucosidosis
ChainA
Resolution2.8 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 FUL A H34 E66 W67 H128 H129 D224 E266 F290 H28 E51 W52 H113 H114 D209 E251 F268
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1odu, PDBe:1odu, PDBj:1odu
PDBsum1odu
PubMed14715651
UniProtQ9WYE2

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