Structure of PDB 1w2t Chain E

Receptor sequence
>1w2tE (length=432) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
LFKPNYHFFPITGWMNDPNGLIFWKGKYHMFYQYNPRKPEWGNICWGHAV
SDDLVHWRHLPVALYPDDETHGVFSGSAVEKDGKMFLVYTYYRDPTHNKG
EKETQCVVMSENGLDFVKYDGNPVISKPPEEGTHAFRDPKVNRSNGEWRM
VLGSGKDEKIGRVLLYTSDDLFHWKYEGAIFEDETTKEIDCPDLVRIGEK
DILIYSITSTNSVLFSMGELKEGKLNVEKRGLLDHGTDFYAAQTFFGTDR
VVVIGWLQSWLRTGLYPTKREGWNGVMSLPRELYVENNELKVKPVDELLA
LRKRKVFETAKSGTFLLDVKENSYEIVCEFSGEIELRMGNESEEVVITKS
RDELIVDTTRSGVSGGEVRKSTVEDEATNRIRAFLDSCSVEFFFNDSIAF
SFRIHPENVYNILSVKSNQVKLEVFELENIWL
3D structure
PDB1w2t Crystal Structure of Inactivated Thermotoga Maritima Invertase in Complex with the Trisaccharide Substrate Raffinose.
ChainE
Resolution1.87 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D17 D190
Catalytic site (residue number reindexed from 1) D17 D190
Enzyme Commision number 3.2.1.26: beta-fructofuranosidase.
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 GLC E R137 E188 T208 R137 E188 T208
BS02 FRU E N16 D17 Q33 W41 F74 S75 D138 Y240 W260 N16 D17 Q33 W41 F74 S75 D138 Y240 W260
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004564 beta-fructofuranosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1w2t, PDBe:1w2t, PDBj:1w2t
PDBsum1w2t
PubMed16411890
UniProtO33833|BFRA_THEMA Beta-fructosidase (Gene Name=bfrA)

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