Structure of PDB 7rig Chain D

Receptor sequence

>7rigD (length=1032) Species: 9606 (Homo sapiens)

SAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLL
SQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGF
LKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQK
LLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLE
INPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEA
YIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNEL
ANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVA
ATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIP
IHVFGTETHMTAIVGMALGHRPIPGKSTTLFSRHTKAIVWGMQTRAVQGM
LDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRK
HPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKK
ADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSR
SGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKM
IVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQACANQ
ASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVP
PPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEM
GIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAG
KDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEG
KLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSK
KPNLILNVAGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSM
GFIGHYLDQKRLKQGLYRHPWDDISYVLPEHM

3D structure

• PDB: 7rig Allosteric role of the citrate synthase homology domain of ATP citrate lyase.
• Chain: D
• Resolution: 2.2 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	Q5B	D	K964 L969 I970 K1017 K1018 L1021	K897 L902 I903 K950 K951 L954
BS02	COA	D	R1085 H1086 P1087 W1088	R1018 H1019 P1020 W1021
BS03	COA	D	I970 M971 I973 G974 R976 N1024	I903 M904 I906 G907 R909 N957
BS04	ADP	D	V56 R65 R66 F110 V111 H113 L215 D216	V55 R64 R65 F109 V110 H112 L214 D215
BS05	Q5B	D	A345 N346 F347 T348 R379 F533 F572 S574 R576 S577 I597 V626 N638	A344 N345 F346 T347 R378 F471 F510 S512 R514 S515 I535 V564 N576
BS06	FLC	D	H900 V904 F935 R986 F1061 R1065	H833 V837 F868 R919 F994 R998

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:7rig, PDBe:7rig, PDBj:7rig
• PDBsum: 7rig
• PubMed: 37076498
• UniProt: P53396|ACLY_HUMAN ATP-citrate synthase (Gene Name=ACLY)