Structure of PDB 3mbf Chain A

Receptor sequence
>3mbfA (length=337) Species: 6035 (Encephalitozoon cuniculi) [Search protein sequence]
MDCDHLLRLGMTAKKILENGKGILAADETPKTLGRRFEKLGITNTEENRR
KFREILFSTKGIERYIGGVILNQETFEQTSGSGVPLTELLKKKGIEIGIK
LDKGLIDYKEKEKISVGLEDLDLRCKSSAFKDATFAKWRSLFYFYDGIPS
EDCINENCSILAKYAIICQKNGLVPIVEPEVFLEGDYSMKRSYEVTRQIL
STLMKYLNYELVYIPGVLIKASYVTSGQLSNEKYTPKKVATFTLRALLST
IPCGIPGIVFLSGGHGSEDAIGFLNAINMERGCRTWSLSFSFARALTDGV
LETWRGDDSNIEEAQKILLETSFKACRGAEGKLWDQE
3D structure
PDB3mbf Structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi.
ChainA
Resolution2.37 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D28 K138 E179 E181 K221 S292
Catalytic site (residue number reindexed from 1) D27 K137 E178 E180 K220 S291
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
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 2FP A A26 D28 E29 T30 T33 K101 K138 E179 K221 S263 G264 A294 R295 A25 D27 E28 T29 T32 K100 K137 E178 K220 S262 G263 A293 R294
Gene Ontology
Molecular Function
GO:0004332 fructose-bisphosphate aldolase activity
GO:0016829 lyase activity
Biological Process
GO:0006096 glycolytic process
GO:0030388 fructose 1,6-bisphosphate metabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:3mbf, PDBe:3mbf, PDBj:3mbf
PDBsum3mbf
PubMed21904050
UniProtQ8SSM8|ALF_ENCCU Fructose-bisphosphate aldolase (Gene Name=ECU01_0240)

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