Structure of PDB 6n2o Chain C

Receptor sequence
>6n2oC (length=572) Species: 156889 (Magnetococcus marinus MC-1) [Search protein sequence]
EKKDLIIRVAGEGGEGIISSGDFIAAACARAGLEVYTFKTFPAEIKGGYA
MYQVRASSEKLYCQGDTFDVFCAFNGEAYEQNKDKIKPGTAFVYDYPGGD
FEPDEIPEGVFAYPIPMSQTAKEMKSYRSKNMVALGALSELFNISENTLK
EVLSDKFGKKGEEVLAFNLEAFDKGKALAKALTKADPFRVADPQEPKDVI
IMAGNDAVGLGGILGGLEFFSAYPITPATEVAKYVATHLPKCGGDLVQAE
DEIASIAQVLGASYAGKKSMTATSGPGLALMSEMLGMAHMSETPCLVVDV
QRGGPSTGLPTKHEQSDLFLAIHGGHGDSPRIVLSVEDVKDCISMTVDGL
NLAEKYQAPVIVLSDGSLAFSTQTIPRPKPEDFTIINRKTWDGQGTYKRY
ELTEDNISPMAAPGTPNAKHIATGLEHGETGAPNYSPANHELMHRKRFNK
QNSVLDFYKNMEVEGVEGEADVGIITWGSTIGVVREAMQRLTAEGLKVKA
MYPKLLWPMPVADYDAFGATCKKVIVPEVNFQGQLSHFIRAETSIKPIPY
TICGGLPFTPEMIVNRVKEEIQ
3D structure
PDB6n2o A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes C-C bonds from CO2.
ChainC
Resolution2.824 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 SCA C G15 G17 I18 I19 S20 F42 A44 E45 I46 R129 N132 F158 N169 T227 R303 G14 G16 I17 I18 S19 F41 A43 E44 I45 R128 N131 F157 N168 T226 R302
BS02 TPP C P225 I226 E253 P224 I225 E252
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016491 oxidoreductase activity
GO:0016903 oxidoreductase activity, acting on the aldehyde or oxo group of donors
Biological Process
GO:0006979 response to oxidative stress

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Molecular Function
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Biological Process
External links
PDB RCSB:6n2o, PDBe:6n2o, PDBj:6n2o
PDBsum6n2o
PubMed31080943
UniProtA0L8G4

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