Structure of PDB 4ffg Chain D

Receptor sequence
>4ffgD (length=480) Species: 37931 (Paenarthrobacter ureafaciens) [Search protein sequence]
AVYHMTPPSGWLCDPQRPVTTHGAYQLYYLHSDQNNGPGGWDHASTTDGV
AFTHHGTVMPLRPDFPVWSGSAVVDTANTAGFGAGAVVALATQPTDGVRK
YQEQYLYWSTDGGFTFTALPDPVIVNTDGRAATTPAEIENAEWFRDPKIH
WDTARGEWVCVIGRLRYAAFYTSPNLRDWTLRRNFDYPNHALGGIECPDL
FEITADDGTRHWVLAASMDAYGIGLPMTYAYWTGTWDGEQFHADDLTPQW
LDWGWDWYAAVTWPSIDAPETKRLAIAWMNNWKYAARDVPTDASDGYNGQ
NSIVRELRLARQPGGWYTLLSTPVAALTNYVTATTTLPDRTVDGSAVLPW
NGRAYEIELDIAWDTATNVGISVGRSPDGTRHTNIGKYGADLYVDRGPSD
LAGYSLAPYSRAAAPIDPGARSVHLRILVDTQSVEVFVNAGHTVLSQQVH
FAEGDTGISLYTDGGPAHFTGIVVREIGQA
3D structure
PDB4ffg Structural and functional basis for substrate specificity and catalysis of levan fructotransferase.
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D54 E236
Catalytic site (residue number reindexed from 1) D14 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 D Y207 N224 Y167 N184
BS02 0U8 D N408 Y428 Y433 D435 R451 D503 N368 Y388 Y393 D395 R411 D463
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:4ffg, PDBe:4ffg, PDBj:4ffg
PDBsum4ffg
PubMed22810228
UniProtQ9KJD0

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