Structure of PDB 6qfb Chain B Binding Site BS02

Receptor Information
>6qfb Chain B (length=1035) 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
IHVFGTETHMTAIVGMALGHRPIPKSTTLFSRHTKAIVWGMQTRAVQGML
DFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKH
PEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKA
DQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRS
GGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMI
VVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGA
CANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPA
QEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVF
KEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIIC
ARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKM
KKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKI
TTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVL
GRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEH
Ligand information
Ligand ID2HP
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-1
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-M
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0OP(=O)(O)[O-]
ACDLabs 10.04[O-]P(=O)(O)O
CACTVS 3.341O[P](O)([O-])=O
FormulaH2 O4 P
NameDIHYDROGENPHOSPHATE ION
ChEMBL
DrugBankDB02831
ZINC
PDB chain6qfb Chain B Residue 1201 [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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PDB6qfb Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.
Resolution3.25 Å
Binding residue
(original residue number in PDB)		G282 G283 S663 G665
Binding residue
(residue number reindexed from 1)		G281 G282 S600 G602
Annotation score1
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
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Cellular Component
External links
PDB RCSB:6qfb, PDBe:6qfb, PDBj:6qfb
PDBsum6qfb
PubMed30944476
UniProtP53396|ACLY_HUMAN ATP-citrate synthase (Gene Name=ACLY)

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