Structure of PDB 4ffi Chain C

Receptor sequence
>4ffiC (length=479) Species: 37931 (Paenarthrobacter ureafaciens) [Search protein sequence]
AVYHMTPPSGWLCNPQRPVTTHGAYQLYYLHSDQNNGPGGWDHASTTDGV
AFTHHGTVMPLRPDFPVWSGSAVVDTANTAGFGAGAVVALATQPTDGVRK
YQEQYLYWSTDGGFTFTALPDPVIVNTDGRAATTPAEIENAEWFRDPKIH
WDTARGEWVCVIGRLRYAAFYTSPNLRDWTLRRNFDYPNHALGGIECPDL
FEITADDGTRHWVLAASMDAYGIGLPMTYAYWTGTWDGEQFHADDLTPQW
LDWGWDWYAAVTWPSIDAPETKRLAIAWMNNWKYAARDVPTDASDGYNGQ
NSIVRELRLARQPGGWYTLLSTPVAALTNYVTATTTLPDRTVDGSAVLPW
NGRAYEIELDIAWDTATNVGISVGRSPDGTRHTNIGKYGADLYVDRGPSD
LAGYSLAPYSRAAAPIDPGARSVHLRILVDTQSVEVFVNAGHTVLSQQVH
FAEGDTGISLYTDGGPAHFTGIVVREIGQ
3D structure
PDB4ffi Structural and functional basis for substrate specificity and catalysis of levan fructotransferase.
ChainC
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) 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 C C53 N54 E236 W322 C13 N14 E196 W282
BS02 FRU C W51 S72 G77 G79 V107 W108 W11 S32 G37 G39 V67 W68
BS03 FRU C D168 R204 Y207 N224 D128 R164 Y167 N184
BS04 FRU C Y207 D226 Y167 D186
BS05 FRU C Y428 Y433 D435 R451 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

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Molecular Function
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Cellular Component
External links
PDB RCSB:4ffi, PDBe:4ffi, PDBj:4ffi
PDBsum4ffi
PubMed22810228
UniProtQ9KJD0

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