Structure of PDB 8g1f Chain B

Receptor sequence

>8g1fB (length=1037) Species: 9606 (Homo sapiens)

SAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLL
SQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGF
LKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQK
LLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLE
INPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEA
YIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNEL
ANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVA
ATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIP
IHVFGTETHMTAIVGMALGHRPIPGKSTTLFSRHTKAIVWGMQTRAVQGM
LDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRK
HPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKK
ADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSR
SGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKM
IVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAG
ACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVP
AQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEV
FKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTII
CARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNK
MKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEK
ITTSKKPNLILNVAGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFV
LGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHM

3D structure

• PDB: 8g1f Allosteric role of the citrate synthase homology domain of ATP citrate lyase.
• Chain: B
• Resolution: 2.4 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	ACO	B	R1085 H1086 P1087 W1088	R1023 H1024 P1025 W1026
BS02	Q5B	B	A280 G309 A345 N346 F347 T348 R379 F533 F572 S574 R576 S577 I597 E599 A624 T625 V626	A279 G308 A344 N345 F346 T347 R378 F471 F510 S512 R514 S515 I535 E537 A562 T563 V564
BS03	ADP	B	V56 R65 R66 P109 F110 V111 L215 D216	V55 R64 R65 P108 F109 V110 L214 D215
BS04	ACO	B	A938 M971 G972 I973 G974 R976 N1024 A1026	A876 M909 G910 I911 G912 R914 N962 A964
BS05	OAA	B	H900 F935 R1065	H838 F873 R1003
BS06	Q5B	B	K964 L969 I970 I973 K1017 L1021	K902 L907 I908 I911 K955 L959

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:8g1f, PDBe:8g1f, PDBj:8g1f
• PDBsum: 8g1f
• PubMed: 37076498
• UniProt: P53396|ACLY_HUMAN ATP-citrate synthase (Gene Name=ACLY)