Structure of PDB 8g1e Chain A

Receptor sequence
>8g1eA (length=1037) Species: 9606 (Homo sapiens) [Search protein sequence]
SAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLL
SQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGF
LKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQK
LLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLE
INPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEA
YIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNEL
ANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVA
ATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIP
IHVFGTETHMTAIVGMALGHRPIPGKSTTLFSRHTKAIVWGMQTRAVQGM
LDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRK
HPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKK
ADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSR
SGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKM
IVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAG
ACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVP
AQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEV
FKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTII
CARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNK
MKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEK
ITTSKKPNLILNVAGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFV
LGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHM
3D structure
PDB8g1e Allosteric role of the citrate synthase homology domain of ATP citrate lyase.
ChainA
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.3.8: ATP citrate synthase.
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 ACO A A938 G972 I973 G974 R976 N1024 A1026 A876 G910 I911 G912 R914 N962 A964
BS02 OAA A H900 R1065 H838 R1003
BS03 ACO A R1085 H1086 P1087 W1088 R1023 H1024 P1025 W1026
BS04 Q5B A K964 L969 I970 I973 K1017 K1018 L1021 K902 L907 I908 I911 K955 K956 L959
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003878 ATP citrate synthase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
Biological Process
GO:0006085 acetyl-CoA biosynthetic process
GO:0006101 citrate metabolic process
GO:0006107 oxaloacetate metabolic process
GO:0006629 lipid metabolic process
GO:0006633 fatty acid biosynthetic process
GO:0006695 cholesterol biosynthetic process
GO:0008610 lipid biosynthetic process
GO:0015936 coenzyme A metabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane
GO:0035578 azurophil granule lumen
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8g1e, PDBe:8g1e, PDBj:8g1e
PDBsum8g1e
PubMed37076498
UniProtP53396|ACLY_HUMAN ATP-citrate synthase (Gene Name=ACLY)

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