Structure of PDB 3u14 Chain A

Receptor sequence

>3u14A (length=509) Species: 27300 (Schwanniomyces occidentalis)

LSVDTSEYNRPLIHFTPEKGWMNAPNGLFYDKTAKLWHLYFQYNPNATAW
GQPLYWGHATSNDLVHWDEHEIAIGPEHDNEGIFSGSIVVDHNNTSGFFN
SSIDPNQRIVAIYTNNIPDNQTQDIAFSLDGGYTFTKYENNPVIDVSSNQ
FRDPKVFWHEDSNQWIMVVSKSQEYKIQIFGSANLKNWVLNSNFSSGYYG
NQYECPGLIEVPIENSDKSKWVMFLAINPGSPLGGSINQYFVGDFDGFQF
VPDDSQTRFVDIGKDFYAFQTFSEVEHGVLGLAWASNWQYADQVPTNPWR
SSTSLARNYTLRYVHTNAETKQLTLIQNPVLPDSINVVDKLKKKNVKLTN
KKPIKTNFKGSTGLFDFNITFKVLNLNVSPGKTHFDILINSQELNSSVDS
IKIGFDSSQSSFYIDRHIPNVEFPRKQFFTDKLAAYLEPLDYDQDLRVFS
LYGIVDKNIIELYFNDGTVAMTNTFFMGEGKYPHDIQIVTDTEEPLFELE
SVIIRELNK

3D structure

• PDB: 3u14 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.
• Chain: A
• Resolution: 2.24 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A50 E230
• Catalytic site (residue number reindexed from 1): A24 E204
• 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	A	W314 D318	W288 D292
BS02	FRU	A	N254 W314	N228 W288
BS03	FRU	A	R178 E230	R152 E204
BS04	FRU	A	N49 Q68 W76 F110 S111 R178 D179 E230	N23 Q42 W50 F84 S85 R152 D153 E204

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:3u14, PDBe:3u14, PDBj:3u14
• PDBsum: 3u14
• PubMed: 22511773
• UniProt: E5D0X5