Structure of PDB 6hxh Chain C

Receptor sequence

>6hxhC (length=1033) Species: 9606 (Homo sapiens)

SAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLL
SQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGF
LKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQK
LLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLE
INPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEA
YIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNEL
ANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVA
ATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIP
IHVFGTETHMTAIVGMALGHRPIKSTTLFSRHTKAIVWGMQTRAVQGMLD
FDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKHP
EVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKAD
QKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSG
GMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIV
VLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGAC
ANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQ
EVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFK
EEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICA
RAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMK
KEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKIT
TSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLG
RSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPE

3D structure

• PDB: 6hxh Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.
• Chain: C
• Resolution: 3.3 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	MG	C	S308 E599	S307 E535
BS02	FLC	C	S308 G309 A345 N346 F347 T348 R379	S307 G308 A344 N345 F346 T347 R378
BS03	COA	C	G261 F533 F572 S574 R576 I597 E599 A624 T625 V626	G260 F469 F508 S510 R512 I533 E535 A560 T561 V562
BS04	ADP	C	V56 K58 R65 R66 F110 V111 H113 E118 G139 V140 P204 L215 D216	V55 K57 R64 R65 F109 V110 H112 E117 G138 V139 P203 L214 D215
BS05	MG	C	N203 D216	N202 D215
BS06	COA	C	K964 L969 I970 I973 K1017 K1018 L1021	K900 L905 I906 I909 K953 K954 L957

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0003878 ATP citrate synthase activity
• GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer

Biological Process

• GO:0006085 acetyl-CoA biosynthetic process
• GO:0006101 citrate metabolic process

External links

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