Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6VUM

Structure of nevanimibe-bound human tetrameric ACAT1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000062	molecular_function	fatty-acyl-CoA binding
A	0004772	molecular_function	sterol O-acyltransferase activity
A	0005515	molecular_function	protein binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006629	biological_process	lipid metabolic process
A	0008202	biological_process	steroid metabolic process
A	0008203	biological_process	cholesterol metabolic process
A	0008374	molecular_function	O-acyltransferase activity
A	0010742	biological_process	macrophage derived foam cell differentiation
A	0010878	biological_process	cholesterol storage
A	0015485	molecular_function	cholesterol binding
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0033344	biological_process	cholesterol efflux
A	0034379	biological_process	very-low-density lipoprotein particle assembly
A	0034383	biological_process	low-density lipoprotein particle clearance
A	0034736	molecular_function	cholesterol O-acyltransferase activity
A	0042632	biological_process	cholesterol homeostasis
A	0042986	biological_process	positive regulation of amyloid precursor protein biosynthetic process
B	0000062	molecular_function	fatty-acyl-CoA binding
B	0004772	molecular_function	sterol O-acyltransferase activity
B	0005515	molecular_function	protein binding
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006629	biological_process	lipid metabolic process
B	0008202	biological_process	steroid metabolic process
B	0008203	biological_process	cholesterol metabolic process
B	0008374	molecular_function	O-acyltransferase activity
B	0010742	biological_process	macrophage derived foam cell differentiation
B	0010878	biological_process	cholesterol storage
B	0015485	molecular_function	cholesterol binding
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0033344	biological_process	cholesterol efflux
B	0034379	biological_process	very-low-density lipoprotein particle assembly
B	0034383	biological_process	low-density lipoprotein particle clearance
B	0034736	molecular_function	cholesterol O-acyltransferase activity
B	0042632	biological_process	cholesterol homeostasis
B	0042986	biological_process	positive regulation of amyloid precursor protein biosynthetic process
C	0000062	molecular_function	fatty-acyl-CoA binding
C	0004772	molecular_function	sterol O-acyltransferase activity
C	0005515	molecular_function	protein binding
C	0005783	cellular_component	endoplasmic reticulum
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006629	biological_process	lipid metabolic process
C	0008202	biological_process	steroid metabolic process
C	0008203	biological_process	cholesterol metabolic process
C	0008374	molecular_function	O-acyltransferase activity
C	0010742	biological_process	macrophage derived foam cell differentiation
C	0010878	biological_process	cholesterol storage
C	0015485	molecular_function	cholesterol binding
C	0016020	cellular_component	membrane
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0033344	biological_process	cholesterol efflux
C	0034379	biological_process	very-low-density lipoprotein particle assembly
C	0034383	biological_process	low-density lipoprotein particle clearance
C	0034736	molecular_function	cholesterol O-acyltransferase activity
C	0042632	biological_process	cholesterol homeostasis
C	0042986	biological_process	positive regulation of amyloid precursor protein biosynthetic process
D	0000062	molecular_function	fatty-acyl-CoA binding
D	0004772	molecular_function	sterol O-acyltransferase activity
D	0005515	molecular_function	protein binding
D	0005783	cellular_component	endoplasmic reticulum
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0006629	biological_process	lipid metabolic process
D	0008202	biological_process	steroid metabolic process
D	0008203	biological_process	cholesterol metabolic process
D	0008374	molecular_function	O-acyltransferase activity
D	0010742	biological_process	macrophage derived foam cell differentiation
D	0010878	biological_process	cholesterol storage
D	0015485	molecular_function	cholesterol binding
D	0016020	cellular_component	membrane
D	0016740	molecular_function	transferase activity
D	0016746	molecular_function	acyltransferase activity
D	0033344	biological_process	cholesterol efflux
D	0034379	biological_process	very-low-density lipoprotein particle assembly
D	0034383	biological_process	low-density lipoprotein particle clearance
D	0034736	molecular_function	cholesterol O-acyltransferase activity
D	0042632	biological_process	cholesterol homeostasis
D	0042986	biological_process	positive regulation of amyloid precursor protein biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue OLA A 701

Chain	Residue
A	PHE258
A	ARG262
A	MET265
A	PHE392
A	LEU428
A	HIS460

site_id	AC2
Number of Residues	3
Details	binding site for residue CLR A 702

Chain	Residue
A	TRP186
A	TRP189
A	ILE190

site_id	AC3
Number of Residues	4
Details	binding site for residue CLR A 703

Chain	Residue
A	ARG272
A	PRO276
A	ASP435
A	TRP438

site_id	AC4
Number of Residues	12
Details	binding site for residue CLR A 704

Chain	Residue
A	ILE138
A	ILE141
A	TYR142
A	PHE145
A	ILE146
A	CYS333
A	TYR336
A	PHE378
A	PHE382
A	TRP408
B	HIS137
B	THR140

site_id	AC5
Number of Residues	7
Details	binding site for residue ROV A 705

Chain	Residue
A	THR380
A	TYR416
A	TRP420
A	ASN421
A	VAL424
A	HIS460
A	COA706

site_id	AC6
Number of Residues	12
Details	binding site for residue COA A 706

Chain	Residue
A	TYR417
A	ARG418
A	HIS425
A	TYR433
A	LYS445
A	MET449
A	VAL452
A	PHE453
A	SER456
A	PHE479
A	ASP492
A	ROV705

site_id	AC7
Number of Residues	11
Details	binding site for residue OLA B 701

Chain	Residue
B	PHE258
B	ILE261
B	ARG262
B	MET265
B	PHE302
B	LEU389
B	VAL424
B	LEU428
B	SER456
B	HIS460
B	ROV705

site_id	AC8
Number of Residues	14
Details	binding site for residue 3VV B 702

Chain	Residue
B	TYR413
B	TYR417
B	ARG418
B	HIS425
B	TYR433
B	MET449
B	VAL452
B	PHE453
B	SER456
B	PHE479
B	PHE486
B	ASP492
B	SER506
B	GLY510

site_id	AC9
Number of Residues	11
Details	binding site for residue CLR B 703

Chain	Residue
A	HIS137
A	THR140
B	ILE141
B	TYR142
B	ILE146
B	LEU149
B	GLY332
B	CYS333
B	PHE378
B	PHE382
B	TRP408

site_id	AD1
Number of Residues	4
Details	binding site for residue CLR B 704

Chain	Residue
B	MET228
B	VAL271
B	PRO276
B	TRP438

site_id	AD2
Number of Residues	5
Details	binding site for residue ROV B 705

Chain	Residue
B	TRP420
B	ASN421
B	SER456
B	HIS460
B	OLA701

site_id	AD3
Number of Residues	6
Details	binding site for residue OLA C 701

Chain	Residue
C	PHE258
C	ARG262
C	MET265
C	PHE392
C	LEU428
C	HIS460

site_id	AD4
Number of Residues	3
Details	binding site for residue CLR C 702

Chain	Residue
C	TRP186
C	TRP189
C	ILE190

site_id	AD5
Number of Residues	4
Details	binding site for residue CLR C 703

Chain	Residue
C	PRO276
C	ASP435
C	TRP438
C	ARG272

site_id	AD6
Number of Residues	11
Details	binding site for residue CLR C 704

Chain	Residue
C	ILE141
C	TYR142
C	PHE145
C	ILE146
C	CYS333
C	TYR336
C	PHE378
C	PHE382
C	TRP408
D	HIS137
D	THR140

site_id	AD7
Number of Residues	7
Details	binding site for residue ROV C 705

Chain	Residue
C	THR380
C	TYR416
C	TRP420
C	ASN421
C	VAL424
C	HIS460
C	COA706

site_id	AD8
Number of Residues	12
Details	binding site for residue COA C 706

Chain	Residue
C	TYR417
C	ARG418
C	HIS425
C	TYR433
C	LYS445
C	MET449
C	VAL452
C	PHE453
C	SER456
C	PHE479
C	ASP492
C	ROV705

site_id	AD9
Number of Residues	11
Details	binding site for residue OLA D 701

Chain	Residue
D	PHE258
D	ILE261
D	ARG262
D	MET265
D	PHE302
D	LEU389
D	VAL424
D	LEU428
D	SER456
D	HIS460
D	ROV705

site_id	AE1
Number of Residues	14
Details	binding site for residue 3VV D 702

Chain	Residue
D	TYR413
D	TYR417
D	ARG418
D	HIS425
D	TYR433
D	MET449
D	VAL452
D	PHE453
D	SER456
D	PHE479
D	PHE486
D	ASP492
D	SER506
D	GLY510

site_id	AE2
Number of Residues	11
Details	binding site for residue CLR D 703

Chain	Residue
C	HIS137
C	THR140
D	ILE141
D	TYR142
D	ILE146
D	LEU149
D	GLY332
D	CYS333
D	PHE378
D	PHE382
D	TRP408

site_id	AE3
Number of Residues	4
Details	binding site for residue CLR D 704

Chain	Residue
D	MET228
D	VAL271
D	PRO276
D	TRP438

site_id	AE4
Number of Residues	5
Details	binding site for residue ROV D 705

Chain	Residue
D	TRP420
D	ASN421
D	SER456
D	HIS460
D	OLA701

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6P2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P2P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	188
Details	Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	100
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6P2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P2P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	420
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	100
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6P2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P2P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	92
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6P2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P2P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	128
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6P2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P2P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	100
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6P2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P2P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	96
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6P2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P2P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	60
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6P2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P2P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	24
Details	Motif: {"description":"FYXDWWN motif","evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"16154994","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16647063","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6P2P","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6P2J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32433613","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32433614","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6P2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P2P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VUM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)