Structure of PDB 7liw Chain B Binding Site BS03

Receptor Information
>7liw Chain B (length=1034) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLL
SQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGF
LKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGAQKLLVGVDEKL
NPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKD
GVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKS
GASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGA
PSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETH
MTAIVGMALGHRPIPNQPPTAGKSTTLFSRHTKAIVWGMQTRAVQGMLDF
DYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKHPE
VDVLINFASLRSAYDSTMETMNYAQIRTIAIIAQGIPEALTRKLIKKADQ
KGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGG
MSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVV
LGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACA
NQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQE
VPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKE
EMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICAR
AGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKK
EGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITT
SKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGR
SMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHM
Ligand information
Ligand IDY2A
InChIInChI=1S/C6H9O10P/c7-3(8)1-6(12,5(10)11)2-4(9)16-17(13,14)15/h12H,1-2H2,(H,7,8)(H,10,11)(H2,13,14,15)/t6-/m0/s1
InChIKeyRAAPFOXFYNTKEB-LURJTMIESA-N
SMILES
SoftwareSMILES
CACTVS 3.385OC(=O)C[C@](O)(CC(=O)O[P](O)(O)=O)C(O)=O
ACDLabs 12.01C(C(CC(=O)OP(O)(O)=O)(C(=O)O)O)C(O)=O
OpenEye OEToolkits 2.0.7C(C(=O)O)C(CC(=O)OP(=O)(O)O)(C(=O)O)O
CACTVS 3.385OC(=O)C[C](O)(CC(=O)O[P](O)(O)=O)C(O)=O
OpenEye OEToolkits 2.0.7C(C(=O)O)[C@](CC(=O)OP(=O)(O)O)(C(=O)O)O
FormulaC6 H9 O10 P
Name(2S)-2-hydroxy-2-[2-oxo-2-(phosphonooxy)ethyl]butanedioic acid
ChEMBL
DrugBank
ZINC
PDB chain7liw Chain B Residue 2003 [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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PDB7liw Reply to: Acetyl-CoA is produced by the citrate synthase homology module of ATP-citrate lyase.
Resolution2.85 Å
Binding residue
(original residue number in PDB)		G281 G282 A345 N346 F347 T348 R379 G665 H760
Binding residue
(residue number reindexed from 1)		G271 G272 A335 N336 F337 T338 R369 G600 H695
Annotation score2
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7liw, PDBe:7liw, PDBj:7liw
PDBsum7liw
PubMed34294921
UniProtP53396|ACLY_HUMAN ATP-citrate synthase (Gene Name=ACLY)

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