Structure of PDB 1fuq Chain B

Receptor sequence

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

MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALAL
TKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQHDDEFPLAIWQTGSGT
QSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHV
AALLALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQE
ISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYARRVADEL
AVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLAS
GPRCGIGEISIPENEPMPGKVNPTQCEALTMLCCQVMGNDVAINMGGASG
NFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNE
SLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWV
RPEQM

3D structure

• PDB: 1fuq Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli.
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N107 T187 H188 K324 E331
• Catalytic site (residue number reindexed from 1): N107 T187 H188 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	SIF	B	R126 H129 P130 D132	R126 H129 P130 D132
BS02	CIT	B	T100 S140	T100 S140

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