Structure of PDB 1fuq Chain A

Receptor sequence
>1fuqA (length=456) Species: 562 (Escherichia coli) [Search protein sequence]
VRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKR
AAAKVNEDLGLLSEEKASAIRQAADEVLAGQHDDEFPLAIWQTGSGTQSN
MNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAAL
LALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISG
WVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYARRVADELAVI
TCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPR
CGIGEISIPENEPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAINMGGAS
GNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLN
ESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSW
VRPEQM
3D structure
PDB1fuq Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N107 T187 H188 S318 K324 E331
Catalytic site (residue number reindexed from 1) N104 T184 H185 S315 K321 E328
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 A R126 H129 P130 N131 D132 R123 H126 P127 N128 D129
BS02 CIT A T100 S139 S140 N141 T97 S136 S137 N138
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1fuq, PDBe:1fuq, PDBj:1fuq
PDBsum1fuq
PubMed8909293
UniProtP05042|FUMC_ECOLI Fumarate hydratase class II (Gene Name=fumC)

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