Structure of PDB 3ekl Chain A

Receptor sequence
>3eklA (length=333) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
PIATPEVYAEMLGQAKQNSYAFPAINCTSSETVNAAIKGFADAGSDGIIQ
FSTGGAEFGSGLGVKDMVTGAVALAEFTHVIAAKYPVNVALHTDHCPKDK
LDSYVRPLLAISAQRVSKGGNPLFQSHMWDGSAVPIDENLAIAQELLKAA
AAAKIILEIEIGVVGGLYTSPEDFEKTIEALGAGEHGKYLLAATFGNVHG
VYKPGNVKLRPDILAQGQQVAAAKLGLPADAKPFDFVFHGGSGSLKSEIE
EALRYGVVKMNVDTDTQYAFTRPIAGHMFTNYDGVLKVDGEVGVKKVYDP
RSYLKKAEASMSQRVVQACNDLHCAGKSLTHHH
3D structure
PDB3ekl Structural basis for catalysis of a tetrameric class IIa fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis
ChainA
Resolution1.51 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D95 H96 H212 H252 N274
Catalytic site (residue number reindexed from 1) D94 H95 H199 H239 N261
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 ZN A H96 H212 H252 H95 H199 H239
BS02 ZN A H344 H346 H331 H333
Gene Ontology
Molecular Function
GO:0004332 fructose-bisphosphate aldolase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0016832 aldehyde-lyase activity
GO:0035375 zymogen binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006096 glycolytic process
Cellular Component
GO:0005576 extracellular region
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ekl, PDBe:3ekl, PDBj:3ekl
PDBsum3ekl
PubMed19167403
UniProtP9WQA3|ALF_MYCTU Fructose-bisphosphate aldolase (Gene Name=fba)

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