Structure of PDB 3u75 Chain D

Receptor sequence
>3u75D (length=512) Species: 27300 (Schwanniomyces occidentalis) [Search protein sequence]
SIDLSVDTSEYNRPLIHFTPEKGWMNDPNGLFYDKTAKLWHLYFQYNPNA
TAWGQPLYWGHATSNDLVHWDEHEIAIGPEHDNEGIFSGSIVVDHNNTSG
FFNSSIDPNQRIVAIYTNNIPDNQTQDIAFSLDGGYTFTKYENNPVIDVS
SNQFRDPKVFWHEDSNQWIMVVSKSQEYKIQIFGSANLKNWVLNSNFSSG
YYGNQYACPGLIEVPIENSDKSKWVMFLAINPGSPLGGSINQYFVGDFDG
FQFVPDDSQTRFVDIGKDFYAFQTFSEVEHGVLGLAWASNWQYADQVPTN
PWRSSTSLARNYTLRYVHTNAETKQLTLIQNPVLPDSINVVDKLKKKNVK
LTNKKPIKTNFKGSTGLFDFNITFKVLNLNVSPGKTHFDILINSQELNSS
VDSIKIGFDSSQSSFYIDRHIPNVEFPRKQFFTDKLAAYLEPLDYDQDLR
VFSLYGIVDKNIIELYFNDGTVAMTNTFFMGEGKYPHDIQIVTDTEEPLF
ELESVIIRELNK
3D structure
PDB3u75 Structural and kinetic insights reveal that the amino acid pair GLN228/ASN254 modulates the transfructosylating specificity of Schwanniomyces occidentalis beta-fructofuranosidase, an enzyme that produces prebiotics.
ChainD
Resolution2.68 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D50 A230
Catalytic site (residue number reindexed from 1) D27 A207
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 FRU D N49 D50 Q68 W76 F110 S111 D179 Y293 W314 N26 D27 Q45 W53 F87 S88 D156 Y270 W291
BS02 FRU D W314 D318 R451 W291 D295 R428
BS03 GLC D W76 D318 W53 D295
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3u75, PDBe:3u75, PDBj:3u75
PDBsum3u75
PubMed22511773
UniProtE5D0X5

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