Structure of PDB 6qfb Chain B

Receptor sequence

>6qfbB (length=1035) Species: 9606 (Homo sapiens)

SAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLL
SQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGF
LKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQK
LLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLE
INPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEA
YIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNEL
ANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVA
ATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIP
IHVFGTETHMTAIVGMALGHRPIPKSTTLFSRHTKAIVWGMQTRAVQGML
DFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKH
PEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKA
DQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRS
GGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMI
VVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGA
CANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPA
QEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVF
KEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIIC
ARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKM
KKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKI
TTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVL
GRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEH

3D structure

• PDB: 6qfb Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.
• Chain: B
• Resolution: 3.25 Å

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	COA	B	F347 S574 R576 S577 E599 A624 T625	F346 S511 R513 S514 E536 A561 T562
BS02	2HP	B	G282 G283 S663 G665	G281 G282 S600 G602
BS03	FLC	B	S308 G309 N346 F347 T348 R379	S307 G308 N345 F346 T347 R378
BS04	COA	B	K964 L969 I970 K1017 K1018 L1021	K901 L906 I907 K954 K955 L958
BS05	ADP	B	V56 K58 R65 R66 G67 V111 H113 E118 P204 L215 D216	V55 K57 R64 R65 G66 V110 H112 E117 P203 L214 D215
BS06	MG	B	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

External links

• PDB: RCSB:6qfb, PDBe:6qfb, PDBj:6qfb
• PDBsum: 6qfb
• PubMed: 30944476
• UniProt: P53396|ACLY_HUMAN ATP-citrate synthase (Gene Name=ACLY)