Structure of PDB 6uql Chain A

Receptor sequence
>6uqlA (length=532) Species: 347515 (Leishmania major strain Friedlin) [Search protein sequence]
DFHFSAIFQPTDPHHHQTEFAKVEGSEKYVEEVEVFGRQALKVNPEALTI
LAHRAFSDVHHFFRKDHLEGWRRAIEDPEASDNDRYVATTLLKNACIAAG
RVLPSCQDTGTAIVLGKRGELCWTGGEDEKYLSKGIWNAYRYHNLRYSQT
AALDMFKECNTGDNLPAQLDLLAVPGSDYEFLFIAKGGGSANKAYLYQET
KALLNPKSLRAFIEEKLKTLGTAACPPYHIALVIGGTSAEMTMKTVKLAS
CRYYDSLPTTGDKYGRAFRDPEWEKIVMEVAQKSGIGAQFGGKYFAHQAR
VIRLPRHGASCPVGLAVSCSADRQILAHINKSGIYIEQLEQNPAQYLPTS
VKVDLKRPIDKVRQQLSQYPVGTRVMLNGTLIVARDIAHAKIKEMMDNGE
PLPEYMKTSPIYYAGPAKTPEGYASGSFGPTTAGAMDSYVDLFQSHGGSY
ITLAKGNRSKQVTDACKKHGGFYLGSIGGPAAILAKDSIKQVTCLAFPEL
GMEAVWKIEVEDFPAFIVVDDKGNDMYSKTLA
3D structure
PDB6uql Structural and Biochemical Investigations of the [4Fe-4S] Cluster-Containing Fumarate Hydratase fromLeishmania major.
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
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 SF4 A C133 D135 G216 A251 C252 C346 A348 K491 C106 D108 G189 A224 C225 C319 A321 K455
Gene Ontology
Molecular Function
GO:0004333 fumarate hydratase activity
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006091 generation of precursor metabolites and energy
GO:0006106 fumarate metabolic process
GO:0006108 malate metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0020015 glycosome
GO:0097014 ciliary plasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6uql, PDBe:6uql, PDBj:6uql
PDBsum6uql
PubMed31743022
UniProtE9AE57|FUM2_LEIMA Fumarate hydratase 2 (Gene Name=FH2)

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