Structure of PDB 6abx Chain A

Receptor sequence
>6abxA (length=370) Species: 399549 (Metallosphaera sedula DSM 5348) [Search protein sequence]
MELRKGLEDIAIKETSITYIDGELGRLYYRGYSIFDLASFSNFEEVAYLL
WYGKLPTRHELDDFKSRLAEERSISEDISTFVKRTAKFGNPMDILRTTVS
MMGLEDRSEGDLIGKAIKMTAKIPTIISLIQRTRRNQEFVEPDPSLSHSE
NFLYMIRGERPSPSDTRVLDVSLMLHMDHEMNASTMACLVVASTLSDIYS
SVVAGISALKGPLHGGANSEALKQFMEIETPDNVEKYVMNKLSSGQRLMG
FGHRIYKTMDPRAKILKEYANQLSKNEEIKRLFEIANRVEEIGIKILGKR
GIYPNVDFYSGLVFYAMGFDPDLFPTIFASARVIGWTAHVDEYLKDNKLI
RPKAIYVGDLGKRYVPIEER
3D structure
PDB6abx Structural insights into the inhibition properties of archaeon citrate synthase from Metallosphaera sedula.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S184 H214 H253 R262 D307
Catalytic site (residue number reindexed from 1) S184 H214 H253 R262 D307
Enzyme Commision number 2.3.3.16: citrate synthase (unknown stereospecificity).
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 FLC A H179 N182 G215 G216 H253 R262 N305 R332 H179 N182 G215 G216 H253 R262 N305 R332 MOAD: Ki=7.19mM
PDBbind-CN: -logKd/Ki=2.14,Ki=7.19mM
Gene Ontology
Molecular Function
GO:0004108 citrate (Si)-synthase activity
GO:0016746 acyltransferase activity
GO:0036440 citrate synthase activity
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006099 tricarboxylic acid cycle
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6abx, PDBe:6abx, PDBj:6abx
PDBsum6abx
PubMed30794680
UniProtA4YGX6

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