Structure of PDB 1fup Chain A

Receptor sequence

>1fupA (length=455) Species: 562 (Escherichia coli)

RSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRA
AAKVNEDLGLLSEEKASAIRQAADEVLAGQHDDEFPLAIWQTGSGTQSNM
NMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALL
ALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGW
VAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYARRVADELAVIT
CAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRC
GIGEISIPENEPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAINMGGASG
NFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNE
SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWV
RPEQM

3D structure

• PDB: 1fup Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli.
• Chain: A
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N107 T187 H188 S318 K324 E331
• Catalytic site (residue number reindexed from 1): N103 T183 H184 S314 K320 E327
• Enzyme Commision number: 4.2.1.2: fumarate hydratase.

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	PMA	A	T100 S139 S140	T96 S135 S136

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004333 fumarate hydratase activity
• GO:0016829 lyase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0006099 tricarboxylic acid cycle
• GO:0006106 fumarate metabolic process
• GO:0006108 malate metabolic process
• GO:0006979 response to oxidative stress

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1fup, PDBe:1fup, PDBj:1fup
• PDBsum: 1fup
• PubMed: 8909293
• UniProt: P05042|FUMC_ECOLI Fumarate hydratase class II (Gene Name=fumC)