Structure of PDB 3elf Chain A

Receptor sequence

>3elfA (length=332) Species: 1773 (Mycobacterium tuberculosis)

PIATPEVYAEMLGQAKQNSYAFPAINCTSSETVNAAIKGFADAGSDGIIQ
FSTGGAEFGSGLGVKDMVTGAVALAEFTHVIAAKYPVNVALHTDHCPKDK
LDSYVRPLLAISAQRVSKGGNPLFQSHMWDGSAVPIDENLAIAQELLKAA
AAAKIILEIEIGVVGGYTSPEDFEKTIEALGAGEHGKYLLAATFGNVHGV
YKPGNVKLRPDILAQGQQVAAAKLGLPADAKPFDFVFHGGSGSLKSEIEE
ALRYGVVKMNVDTDTQYAFTRPIAGHMFTNYDGVLKVDGEVGVKKVYDPR
SYLKKAEASMSQRVVQACNDLHCAGKSLTHHH

3D structure

• PDB: 3elf Structural basis for catalysis of a tetrameric class IIa fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis
• Chain: A
• Resolution: 1.31 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D95 H96 H212 H252 N274
• Catalytic site (residue number reindexed from 1): D94 H95 H198 H238 N260
• 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	N27 S53 D95 H96 H212 G213 H252 G253 S255 N274 V275 D276 T277	N26 S52 D94 H95 H198 G199 H238 G239 S241 N260 V261 D262 T263
BS02	ZN	A	H96 H212 H252	H95 H198 H238
BS03	ZN	A	H344 H346	H330 H332

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