Structure of PDB 6qfb Chain D

Receptor sequence
>6qfbD (length=1025) Species: 9606 (Homo sapiens) [Search protein sequence]
SAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLL
SQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGF
LKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQK
LLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLE
INPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEA
YIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNEL
ANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVA
ATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIP
IHVFGTETHMTAIVGMALGHRPIPKSTTLFSRHTKAIVWGMQTRAVQGML
DFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKH
PEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKA
DQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRS
GGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMI
VVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSQASETAVAKN
QALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYS
WARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLL
WFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTS
GLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHR
VKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPNLILNVD
GLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQ
KRLKQGLYRHPWDDISYVLPEHMSM
3D structure
PDB6qfb Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.
ChainD
Resolution3.25 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 2HP D G283 S663 G665 G282 S600 G602
BS02 COA D K964 L969 I970 K1017 K1018 L1021 K888 L893 I894 K941 K942 L945
BS03 ADP D V56 K58 R65 R66 G67 F110 V111 H113 E118 P204 L215 D216 V55 K57 R64 R65 G66 F109 V110 H112 E117 P203 L214 D215
BS04 MG D N203 D216 N202 D215
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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