Structure of PDB 3pff Chain A

Receptor sequence
>3pffA (length=735) Species: 9606 (Homo sapiens) [Search protein sequence]
SAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLL
SQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGF
LKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQK
LLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLE
INPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEA
YIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNEL
ANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVA
ATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIP
IHVFGTETHMTAIVGMALGHRPIPGKSTTLFSRHTKAIVWGMQTRAVQGM
LDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRK
HPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKK
ADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSR
SGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKM
IVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMQASETAVAKNQ
ALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVP
3D structure
PDB3pff ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E718
Catalytic site (residue number reindexed from 1) E656
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 A D257 S260 A262 D256 S259 A261
BS02 MG A N203 D216 N202 D215
BS03 ADP A V56 K58 R65 R66 G67 F110 V111 H113 E118 V140 P204 L215 D216 V55 K57 R64 R65 G66 F109 V110 H112 E117 V139 P203 L214 D215
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer

View graph for
Molecular Function
External links
PDB RCSB:3pff, PDBe:3pff, PDBj:3pff
PDBsum3pff
PubMed22102020
UniProtP53396|ACLY_HUMAN ATP-citrate synthase (Gene Name=ACLY)

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