6UV5

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0003878	molecular_function	ATP citrate synthase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005576	cellular_component	extracellular region
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006085	biological_process	acetyl-CoA biosynthetic process
A	0006101	biological_process	citrate metabolic process
A	0006107	biological_process	oxaloacetate metabolic process
A	0006629	biological_process	lipid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006695	biological_process	cholesterol biosynthetic process
A	0008610	biological_process	lipid biosynthetic process
A	0015936	biological_process	coenzyme A metabolic process
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0035578	cellular_component	azurophil granule lumen
A	0036064	cellular_component	ciliary basal body
A	0046872	molecular_function	metal ion binding
A	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer
A	0070062	cellular_component	extracellular exosome
A	0110076	biological_process	negative regulation of ferroptosis
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0003878	molecular_function	ATP citrate synthase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005576	cellular_component	extracellular region
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006085	biological_process	acetyl-CoA biosynthetic process
B	0006101	biological_process	citrate metabolic process
B	0006107	biological_process	oxaloacetate metabolic process
B	0006629	biological_process	lipid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0006695	biological_process	cholesterol biosynthetic process
B	0008610	biological_process	lipid biosynthetic process
B	0015936	biological_process	coenzyme A metabolic process
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0035578	cellular_component	azurophil granule lumen
B	0036064	cellular_component	ciliary basal body
B	0046872	molecular_function	metal ion binding
B	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer
B	0070062	cellular_component	extracellular exosome
B	0110076	biological_process	negative regulation of ferroptosis
B	1904813	cellular_component	ficolin-1-rich granule lumen
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0003878	molecular_function	ATP citrate synthase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005576	cellular_component	extracellular region
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006085	biological_process	acetyl-CoA biosynthetic process
C	0006101	biological_process	citrate metabolic process
C	0006107	biological_process	oxaloacetate metabolic process
C	0006629	biological_process	lipid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
C	0006695	biological_process	cholesterol biosynthetic process
C	0008610	biological_process	lipid biosynthetic process
C	0015936	biological_process	coenzyme A metabolic process
C	0016020	cellular_component	membrane
C	0016740	molecular_function	transferase activity
C	0035578	cellular_component	azurophil granule lumen
C	0036064	cellular_component	ciliary basal body
C	0046872	molecular_function	metal ion binding
C	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer
C	0070062	cellular_component	extracellular exosome
C	0110076	biological_process	negative regulation of ferroptosis
C	1904813	cellular_component	ficolin-1-rich granule lumen
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0003878	molecular_function	ATP citrate synthase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005576	cellular_component	extracellular region
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006085	biological_process	acetyl-CoA biosynthetic process
D	0006101	biological_process	citrate metabolic process
D	0006107	biological_process	oxaloacetate metabolic process
D	0006629	biological_process	lipid metabolic process
D	0006633	biological_process	fatty acid biosynthetic process
D	0006695	biological_process	cholesterol biosynthetic process
D	0008610	biological_process	lipid biosynthetic process
D	0015936	biological_process	coenzyme A metabolic process
D	0016020	cellular_component	membrane
D	0016740	molecular_function	transferase activity
D	0035578	cellular_component	azurophil granule lumen
D	0036064	cellular_component	ciliary basal body
D	0046872	molecular_function	metal ion binding
D	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer
D	0070062	cellular_component	extracellular exosome
D	0110076	biological_process	negative regulation of ferroptosis
D	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue ACO A 1201

Chain	Residue
A	PHE533
A	VAL626
A	OAA1203
C	LYS964
C	LEU969
C	ILE970
C	ILE973
C	LYS1017
C	LYS1018
C	LEU1021
A	PHE572
A	ALA573
A	SER574
A	ARG576
A	SER577
A	ILE597
A	GLU599
A	THR625

---

site_id	AC2
Number of Residues	22
Details	binding site for residue ACO A 1202

Chain	Residue
A	ALA938
A	LYS964
A	LEU969
A	ILE970
A	MET971
A	GLY972
A	ILE973
A	GLY974
A	LYS1018
A	LEU1021
A	ASN1024
A	OAA1204
C	TYR531
C	PHE572
C	ALA573
C	SER574
C	ARG576
C	ILE597
C	THR625
C	VAL626
C	GLY665
C	OAA1202

---

site_id	AC3
Number of Residues	5
Details	binding site for residue OAA A 1203

Chain	Residue
A	ALA310
A	ASN346
A	PHE347
A	THR348
A	ACO1201

---

site_id	AC4
Number of Residues	7
Details	binding site for residue OAA A 1204

Chain	Residue
A	HIS900
A	PHE935
A	GLY936
A	ASP1026
A	PHE1061
A	ARG1065
A	ACO1202

---

site_id	AC5
Number of Residues	16
Details	binding site for residue ACO B 1201

Chain	Residue
B	PHE533
B	PHE572
B	ALA573
B	SER574
B	ARG576
B	SER577
B	ILE597
B	GLU599
B	THR625
D	LYS964
D	LEU969
D	ILE970
D	ILE973
D	LYS1017
D	LYS1018
D	LEU1021

---

site_id	AC6
Number of Residues	1
Details	binding site for residue OAA B 1202

Chain	Residue
B	ASN638

---

site_id	AC7
Number of Residues	5
Details	binding site for residue OAA B 1203

Chain	Residue
B	HIS900
B	VAL904
B	PHE935
B	GLY936
B	ASP1026

---

site_id	AC8
Number of Residues	5
Details	binding site for residue OAA C 1201

Chain	Residue
C	HIS900
C	VAL904
C	PHE935
C	ASP1026
D	ARG1085

---

site_id	AC9
Number of Residues	4
Details	binding site for residue OAA C 1202

Chain	Residue
A	ACO1202
C	GLY309
C	ASN346
C	THR348

---

site_id	AD1
Number of Residues	17
Details	binding site for residue ACO D 1201

Chain	Residue
D	OAA1203
B	LYS964
B	LEU969
B	ILE970
B	ILE973
B	LYS1017
B	LYS1018
B	LEU1021
D	ASN346
D	PHE533
D	PHE572
D	SER574
D	ARG576
D	SER577
D	GLU599
D	ALA624
D	THR625

---

site_id	AD2
Number of Residues	7
Details	binding site for residue OAA D 1202

Chain	Residue
C	ARG1085
D	HIS900
D	VAL904
D	GLY936
D	ASP1026
D	PHE1061
D	ARG1065

---

site_id	AD3
Number of Residues	5
Details	binding site for residue OAA D 1203

Chain	Residue
D	ASN346
D	PHE347
D	THR348
D	ASN638
D	ACO1201

---

Functional Information from PROSITE/UniProt

site_id	PS00399
Number of Residues	17
Details	SUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GtcAtmfssevQFGHAG

Chain	Residue	Details
A	GLY746-GLY762

---

site_id	PS01216
Number of Residues	30
Details	SUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGGMSnElnniisrttdGvyegVAIGGD

Chain	Residue	Details
A	SER661-ASP690

---

site_id	PS01217
Number of Residues	25
Details	SUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GrIwtMvAGGGASvvysDtIcdl.GG

Chain	Residue	Details
A	GLY273-GLY297

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1044
Details	Domain: {"description":"ATP-grasp"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22102020","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20558738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22102020","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20558738","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	40
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q91V92","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23932781","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23932781","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91V92","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	16
Details	Cross-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"}]}

Chain

Residue

Details

---