Structure of PDB 3qrh Chain A

Receptor sequence
>3qrhA (length=337) Species: 6035 (Encephalitozoon cuniculi) [Search protein sequence]
MDCDHLLRLGMTAKKILENGKGILAADETPKTLGRRFEKLGITNTEENRR
KFREILFSTKGIERYIGGVILNQETFEQTSGSGVPLTELLKKKGIEIGIK
LDKGLIDYKEKEKISVGLEDLDLRCKSSAFKDATFAKWRSLFYFYDGIPS
EDCINENCSILAKYAIICQKNGLVPIVEPEVFLEGDYSMKRSYEVTRQIL
STLMKYLNYELVYIPGVLIKASYVTSGQLSNEKYTPKKVATFTLRALLST
IPCGIPGIVFLSGGHGSEDAIGFLNAINMERGCRTWSLSFSFARALTDGV
LETWRGDDSNIEEAQKILLETSFKACRGAEGKLWDQE
3D structure
PDB3qrh Crystal structure of fructose bisphosphate aldolase from Encephalitozoon Cuniculi, bound to glyceraldehyde 3-phosphate
ChainA
Resolution2.0 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 G3H A A26 D28 K138 K221 S263 G264 F293 A294 R295 A25 D27 K137 K220 S262 G263 F292 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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Biological Process
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Cellular Component
External links
PDB RCSB:3qrh, PDBe:3qrh, PDBj:3qrh
PDBsum3qrh
PubMed
UniProtQ8SSM8|ALF_ENCCU Fructose-bisphosphate aldolase (Gene Name=ECU01_0240)

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