Structure of PDB 4ffi Chain B

Receptor sequence

>4ffiB (length=480) Species: 37931 (Paenarthrobacter ureafaciens)

AVYHMTPPSGWLCNPQRPVTTHGAYQLYYLHSDQNNGPGGWDHASTTDGV
AFTHHGTVMPLRPDFPVWSGSAVVDTANTAGFGAGAVVALATQPTDGVRK
YQEQYLYWSTDGGFTFTALPDPVIVNTDGRAATTPAEIENAEWFRDPKIH
WDTARGEWVCVIGRLRYAAFYTSPNLRDWTLRRNFDYPNHALGGIECPDL
FEITADDGTRHWVLAASMDAYGIGLPMTYAYWTGTWDGEQFHADDLTPQW
LDWGWDWYAAVTWPSIDAPETKRLAIAWMNNWKYAARDVPTDASDGYNGQ
NSIVRELRLARQPGGWYTLLSTPVAALTNYVTATTTLPDRTVDGSAVLPW
NGRAYEIELDIAWDTATNVGISVGRSPDGTRHTNIGKYGADLYVDRGPSD
LAGYSLAPYSRAAAPIDPGARSVHLRILVDTQSVEVFVNAGHTVLSQQVH
FAEGDTGISLYTDGGPAHFTGIVVREIGQA

3D structure

• PDB: 4ffi Structural and functional basis for substrate specificity and catalysis of levan fructotransferase.
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N54 E236
• Catalytic site (residue number reindexed from 1): N14 E196
• Enzyme Commision number: 4.2.2.16: levan fructotransferase (DFA-IV-forming).

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	B	D168 Y207 N224	D128 Y167 N184
BS02	FRU	B	N408 Y433 D435 R451	N368 Y393 D395 R411
BS03	FRU	B	Y501 D503	Y461 D463
BS04	FRU	B	S385 S412	S345 S372

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0004575 sucrose alpha-glucosidase activity
• GO:0016740 transferase activity
• GO:0016798 hydrolase activity, acting on glycosyl bonds

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0005987 sucrose catabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:4ffi, PDBe:4ffi, PDBj:4ffi
• PDBsum: 4ffi
• PubMed: 22810228
• UniProt: Q9KJD0