Structure of PDB 3ekz Chain A

Receptor sequence

>3ekzA (length=334) Species: 1773 (Mycobacterium tuberculosis)

PIATPEVYAEMLGQAKQNSYAFPAINCTSSETVNAAIKGFADAGSDGIIQ
FSTGGAEFGSGLGVKDMVTGAVALAEFTHVIAAKYPVNVALHTDHCPKDK
LDSYVRPLLAISAQRVSKGGNPLFQSHMWDGSAVPIDENLAIAQELLKAA
AAAKIILEIEIGVVGGKLYTSPEDFEKTIEALGAGEHGKYLLAATFGNVH
GVYKPGNVKLRPDILAQGQQVAAAKLGLPADAKPFDFVFHGGSGSLKSEI
EEALRYGVVKMNVDTDTQYAFTRPIAGHMFTNYDGVLKVDGEVGVKKVYD
PRSYLKKAEASMSQRVVQACNDLHCAGKSLTHHH

3D structure

• PDB: 3ekz Structural basis for catalysis of a tetrameric class IIa fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis
• Chain: A
• Resolution: 2.07 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D95 H96 H212 H252 N274
• Catalytic site (residue number reindexed from 1): D94 H95 H200 H240 N262
• 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	G3P	A	S53 H212 D276	S52 H200 D264
BS02	ZN	A	H96 H212 H252	H95 H200 H240
BS03	ZN	A	H344 H346	H332 H334

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

External links

• PDB: RCSB:3ekz, PDBe:3ekz, PDBj:3ekz
• PDBsum: 3ekz
• PubMed: 19167403
• UniProt: P9WQA3|ALF_MYCTU Fructose-bisphosphate aldolase (Gene Name=fba)