Structure of PDB 4ffh Chain B

Receptor sequence

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

AVYHMTPPSGWLCNPQRPVTTHGAYQLYYLHSDQNNGPGGWDHASTTDGV
AFTHHGTVMPLRPDFPVWSGSAVVDTANTAGFGAGAVVALATQPTDGVRK
YQEQYLYWSTDGGFTFTALPDPVIVNTDGRAATTPAEIENAEWFRDPKIH
WDTARGEWVCVIGRLRYAAFYTSPNLRDWTLRRNFDYPNHALGGIECPDL
FEITADDGTRHWVLAASMDAYGIGLPMTYAYWTGTWDGEQFHADDLTPQW
LDWGWDWYAAVTWPSIDAPETKRLAIAWMNNWKYAARDVPTDASDGYNGQ
NSIVRELRLARQPGGWYTLLSTPVAALTNYVTATTTLPDRTVDGSAVLPW
NGRAYEIELDIAWDTATNVGISVGRSPDGTRHTNIGKYGADLYVDRGPSD
LAGYSLAPYSRAAAPIDPGARSVHLRILVDTQSVEVFVNAGHTVLSQQVH
FAEGDTGISLYTDGGPAHFTGIVVREIGQA

3D structure

• PDB: 4ffh Structural and functional basis for substrate specificity and catalysis of levan fructotransferase.
• Chain: B
• Resolution: 2.2 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	GLC	B	W108 R139 R185 E236	W68 R99 R145 E196
BS02	FRU	B	N54 W108 S109 R185 D186 E236 Y298	N14 W68 S69 R145 D146 E196 Y258
BS03	FRU	B	N408 N424 Y428 Y433 D435 R451	N368 N384 Y388 Y393 D395 R411

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:4ffh, PDBe:4ffh, PDBj:4ffh
• PDBsum: 4ffh
• PubMed: 22810228
• UniProt: Q9KJD0