Structure of PDB 6hxh Chain D

Receptor sequence

>6hxhD (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: D
• 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	COA	D	K964 L969 I970 I973 L1021	K900 L905 I906 I909 L957
BS02	MG	D	S308 E599	S307 E535
BS03	FLC	D	S308 G309 A345 N346 F347 T348 R379	S307 G308 A344 N345 F346 T347 R378
BS04	COA	D	G261 F347 F572 S574 R576 S577 I597 E599 A624 T625 V626	G260 F346 F508 S510 R512 S513 I533 E535 A560 T561 V562
BS05	ADP	D	V56 K58 R65 R66 G67 F110 V111 H113 E118 V140 N203 P204 L215 D216	V55 K57 R64 R65 G66 F109 V110 H112 E117 V139 N202 P203 L214 D215
BS06	MG	D	N203 D216	N202 D215

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)