Structure of PDB 7liw Chain B

Receptor sequence

>7liwB (length=1034) Species: 9606 (Homo sapiens)

SAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLL
SQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGF
LKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGAQKLLVGVDEKL
NPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKD
GVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKS
GASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGA
PSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETH
MTAIVGMALGHRPIPNQPPTAGKSTTLFSRHTKAIVWGMQTRAVQGMLDF
DYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKHPE
VDVLINFASLRSAYDSTMETMNYAQIRTIAIIAQGIPEALTRKLIKKADQ
KGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGG
MSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVV
LGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACA
NQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQE
VPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKE
EMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICAR
AGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKK
EGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITT
SKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGR
SMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHM

3D structure

• PDB: 7liw Reply to: Acetyl-CoA is produced by the citrate synthase homology module of ATP-citrate lyase.
• Chain: B
• Resolution: 2.85 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	ADP	B	V56 R65 R66 E108 F110 V111 H113 L215 D216	V55 R64 R65 E107 F109 V110 H112 L205 D206
BS02	COA	B	F347 F572 S574 R576 S577 I597 A624 T625	F337 F507 S509 R511 S512 I532 A559 T560
BS03	Y2A	B	G281 G282 A345 N346 F347 T348 R379 G665 H760	G271 G272 A335 N336 F337 T338 R369 G600 H695

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:7liw, PDBe:7liw, PDBj:7liw
• PDBsum: 7liw
• PubMed: 34294921
• UniProt: P53396|ACLY_HUMAN ATP-citrate synthase (Gene Name=ACLY)