7LIW

Local refinement of human ATP citrate lyase E599Q mutant ASH domain

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	14
Details	binding site for residue ADP B 2001

Chain	Residue
B	VAL56
B	GLU118
B	GLY139
B	ASN203
B	LEU215
B	ASP216
B	ARG65
B	ARG66
B	GLY67
B	GLU108
B	PRO109
B	PHE110
B	VAL111
B	HIS113

---

site_id	AC2
Number of Residues	20
Details	binding site for residue COA B 2002

Chain	Residue
B	GLY261
B	GLY309
B	PHE347
B	PHE572
B	ALA573
B	SER574
B	ARG576
B	SER577
B	ILE597
B	GLN599
B	ALA624
B	THR625
B	Y2A2003
D	LYS964
D	LEU969
D	ILE970
D	ILE973
D	LYS1017
D	LYS1018
D	LEU1021

---

site_id	AC3
Number of Residues	16
Details	binding site for residue Y2A B 2003

Chain	Residue
B	ALA280
B	GLY281
B	GLY282
B	GLY283
B	SER308
B	SER343
B	ALA345
B	ASN346
B	PHE347
B	THR348
B	ARG379
B	SER663
B	GLY664
B	GLY665
B	HIS760
B	COA2002

---

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	5
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
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_FI3
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_FI4
Number of Residues	1
Details	Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"1371749","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22102020","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	3
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_FI7
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20558738","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	10
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q91V92","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23932781","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
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_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	1
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_FI15
Number of Residues	4
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

---