Structure of PDB 1fua Chain A

Receptor sequence

>1fuaA (length=206) Species: 562 (Escherichia coli)

MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKL
TESHIVFIDGNGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTA
VSILNRSIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKAT
LLQHHGLIACEVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIA
VVLEKF

3D structure

• PDB: 1fua Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli.
• Chain: A
• Resolution: 1.92 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E73 H92 H94 Y113 A117 H155
• Catalytic site (residue number reindexed from 1): E73 H92 H94 Y113 A117 H155
• Enzyme Commision number: 4.1.2.17: L-fuculose-phosphate 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	E73 H92 H94 H155	E73 H92 H94 H155

Gene Ontology

Molecular Function

• GO:0008270 zinc ion binding
• GO:0008738 L-fuculose-phosphate aldolase activity
• GO:0016829 lyase activity
• GO:0016830 carbon-carbon lyase activity
• GO:0016832 aldehyde-lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0005996 monosaccharide metabolic process
• GO:0006004 fucose metabolic process
• GO:0019317 fucose catabolic process
• GO:0019323 pentose catabolic process
• GO:0019568 arabinose catabolic process
• GO:0019571 D-arabinose catabolic process
• GO:0042355 L-fucose catabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1fua, PDBe:1fua, PDBj:1fua
• PDBsum: 1fua
• PubMed: 15299567
• UniProt: P0AB87|FUCA_ECOLI L-fuculose phosphate aldolase (Gene Name=fucA)