Structure of PDB 7rmp Chain C Binding Site BS03

Receptor Information
>7rmp Chain C (length=1032) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLL
SQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGF
LKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQK
LLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLE
INPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEA
YIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNEL
ANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVA
ATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIP
IHVFGTETHMTAIVGMALGHRPIPGKSTTLFSRHTKAIVWGMQTRAVQGM
LDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRK
HPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKK
ADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSR
SGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKM
IVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQACANQ
ASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVP
PPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEM
GIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAG
KDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEG
KLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSK
KPNLILNVAGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSM
GFIGHYLDQKRLKQGLYRHPWDDISYVLPEHM
Ligand information
Ligand IDFLC
InChIInChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12)/p-3
InChIKeyKRKNYBCHXYNGOX-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341OC(CC([O-])=O)(CC([O-])=O)C([O-])=O
OpenEye OEToolkits 1.5.0C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
ACDLabs 10.04O=C([O-])CC(O)(C([O-])=O)CC(=O)[O-]
FormulaC6 H5 O7
NameCITRATE ANION
ChEMBL
DrugBank
ZINC
PDB chain7rmp Chain C Residue 2102 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB7rmp Allosteric role of the citrate synthase homology domain of ATP citrate lyase.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		H900 G936 F1061 R1065
Binding residue
(residue number reindexed from 1)		H833 G869 F994 R998
Annotation score5
Enzymatic activity
Enzyme Commision number 2.3.3.8: ATP citrate synthase.
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
View graph for
Cellular Component
External links
PDB RCSB:7rmp, PDBe:7rmp, PDBj:7rmp
PDBsum7rmp
PubMed37076498
UniProtP53396|ACLY_HUMAN ATP-citrate synthase (Gene Name=ACLY)

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