Structure of PDB 1ixe Chain B

Receptor sequence
>1ixeB (length=370) Species: 274 (Thermus thermophilus) [Search protein sequence]
VARGLEGVLFTESRMCYIDGQQGKLYYYGIPIQELAEKSSFEETTFLLLH
GRLPRRQELEEFSAALARRRALPAHLLESFKRYPVSAHPMSFLRTAVSEF
GMLDPTEGDISREALYEKGLDLIAKFATIVAANKRLKEGKEPIPPREDLS
HAANFLYMANGVEPSPEQARLMDAALILHAEHGFNASTFTAIAAFSTETD
LYSAITAAVASLKGPRHGGANEAVMRMIQEIGTPERAREWVREKLAKKER
IMGMGHRVYKAFDPRAGVLEKLARLVAESKEYQILKIVEEEAGKVLNPRG
IYPNVDFYSGVVYSDLGFSLEFFTPIFAVARISGWVGHILEYQELDNRLL
RPGAKYVGELDVPYVPLEAR
3D structure
PDB1ixe Structural comparison between the open and closed forms of citrate synthase from Thermus thermophilus HB8.
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S189 H219 H258 R267 D312
Catalytic site (residue number reindexed from 1) S187 H217 H256 R265 D306
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 COA B R218 A222 R252 I253 G255 M256 G257 R259 L302 I307 N310 D312 R216 A220 R250 I251 G253 M254 G255 R257 L296 I301 N304 D306
Gene Ontology
Molecular Function
GO:0004108 citrate (Si)-synthase activity
GO:0016740 transferase 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:1ixe, PDBe:1ixe, PDBj:1ixe
PDBsum1ixe
PubMed27493854
UniProtQ5SIM6

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