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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6UI9

Structure of human ATP citrate lyase in complex with acetyl-CoA and oxaloacetate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003878molecular_functionATP citrate synthase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0006085biological_processacetyl-CoA biosynthetic process
A0006101biological_processcitrate metabolic process
A0006107biological_processoxaloacetate metabolic process
A0006629biological_processlipid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006695biological_processcholesterol biosynthetic process
A0008610biological_processlipid biosynthetic process
A0015936biological_processcoenzyme A metabolic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0035578cellular_componentazurophil granule lumen
A0046872molecular_functionmetal ion binding
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
A0070062cellular_componentextracellular exosome
A0110076biological_processnegative regulation of ferroptosis
A1904813cellular_componentficolin-1-rich granule lumen
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003878molecular_functionATP citrate synthase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0006085biological_processacetyl-CoA biosynthetic process
B0006101biological_processcitrate metabolic process
B0006107biological_processoxaloacetate metabolic process
B0006629biological_processlipid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006695biological_processcholesterol biosynthetic process
B0008610biological_processlipid biosynthetic process
B0015936biological_processcoenzyme A metabolic process
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0035578cellular_componentazurophil granule lumen
B0046872molecular_functionmetal ion binding
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0070062cellular_componentextracellular exosome
B0110076biological_processnegative regulation of ferroptosis
B1904813cellular_componentficolin-1-rich granule lumen
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0003878molecular_functionATP citrate synthase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005576cellular_componentextracellular region
C0005829cellular_componentcytosol
C0006085biological_processacetyl-CoA biosynthetic process
C0006101biological_processcitrate metabolic process
C0006107biological_processoxaloacetate metabolic process
C0006629biological_processlipid metabolic process
C0006633biological_processfatty acid biosynthetic process
C0006695biological_processcholesterol biosynthetic process
C0008610biological_processlipid biosynthetic process
C0015936biological_processcoenzyme A metabolic process
C0016020cellular_componentmembrane
C0016740molecular_functiontransferase activity
C0035578cellular_componentazurophil granule lumen
C0046872molecular_functionmetal ion binding
C0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
C0070062cellular_componentextracellular exosome
C0110076biological_processnegative regulation of ferroptosis
C1904813cellular_componentficolin-1-rich granule lumen
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0003878molecular_functionATP citrate synthase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005576cellular_componentextracellular region
D0005829cellular_componentcytosol
D0006085biological_processacetyl-CoA biosynthetic process
D0006101biological_processcitrate metabolic process
D0006107biological_processoxaloacetate metabolic process
D0006629biological_processlipid metabolic process
D0006633biological_processfatty acid biosynthetic process
D0006695biological_processcholesterol biosynthetic process
D0008610biological_processlipid biosynthetic process
D0015936biological_processcoenzyme A metabolic process
D0016020cellular_componentmembrane
D0016740molecular_functiontransferase activity
D0035578cellular_componentazurophil granule lumen
D0046872molecular_functionmetal ion binding
D0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
D0070062cellular_componentextracellular exosome
D0110076biological_processnegative regulation of ferroptosis
D1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00399
Number of Residues17
DetailsSUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GtcAtmfssevQFGHAG
ChainResidueDetails
AGLY746-GLY762
site_idPS01216
Number of Residues30
DetailsSUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGGMSnElnniisrttdGvyegVAIGGD
ChainResidueDetails
ASER661-ASP690
site_idPS01217
Number of Residues25
DetailsSUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GrIwtMvAGGGASvvysDtIcdl.GG
ChainResidueDetails
AGLY273-GLY297
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1044
DetailsDomain: {"description":"ATP-grasp"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22102020","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20558738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22102020","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20558738","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues40
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q91V92","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23932781","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23932781","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91V92","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues16
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"27664236","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23932781","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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