Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6P2J

Dimeric structure of 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	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	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	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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue 3VV A 700

Chain	Residue
A	TRP407
A	VAL452
A	PHE453
A	SER456
A	HIS460
A	ASN415
A	TYR417
A	TRP420
A	ASN421
A	HIS425
A	TYR429
A	TYR433
A	LYS445

site_id	AC2
Number of Residues	19
Details	binding site for residue 3VV B 700

Chain	Residue
B	TRP407
B	SER414
B	ASN415
B	TYR417
B	TRP420
B	ASN421
B	HIS425
B	LEU428
B	TYR429
B	TYR433
B	LYS445
B	MET449
B	VAL452
B	PHE453
B	SER456
B	HIS460
B	PHE476
B	PHE479
B	MET480

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	484
Details	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
A	MET1-ILE138
B	ASN491-LYS496
A	ALA207-ILE218
A	ARG277-ARG319
A	LEU396-ARG443
A	ASN491-LYS496
B	MET1-ILE138
B	ALA207-ILE218
B	ARG277-ARG319
B	LEU396-ARG443

site_id	SWS_FT_FI2
Number of Residues	42
Details	TRANSMEM: Helical; Name=1 => ECO:0000269\|PubMed:32433614, ECO:0000305\|PubMed:32433613, ECO:0007744\|PDB:6P2J, ECO:0007744\|PDB:6P2P, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	ARG139-ASP160
B	ARG139-ASP160

site_id	SWS_FT_FI3
Number of Residues	136
Details	TOPO_DOM: Lumenal => ECO:0000305

Chain	Residue	Details
A	TYR161-LYS180
B	PRO529-PHE550
A	ALA245-SER252
A	LYS353-SER369
A	SER469-VAL474
A	PRO529-PHE550
B	TYR161-LYS180
B	ALA245-SER252
B	LYS353-SER369
B	SER469-VAL474

site_id	SWS_FT_FI4
Number of Residues	50
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:32433614, ECO:0000305\|PubMed:32433613, ECO:0007744\|PDB:6P2J, ECO:0007744\|PDB:6P2P, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	PHE181-TRP206
B	PHE181-TRP206

site_id	SWS_FT_FI5
Number of Residues	50
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:32433614, ECO:0000305\|PubMed:32433613, ECO:0007744\|PDB:6P2J, ECO:0007744\|PDB:6P2P, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	ARG219-LEU244
B	ARG219-LEU244

site_id	SWS_FT_FI6
Number of Residues	46
Details	TRANSMEM: Helical; Name=4 => ECO:0000269\|PubMed:32433614, ECO:0000305\|PubMed:32433613, ECO:0007744\|PDB:6P2J, ECO:0007744\|PDB:6P2P, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	ARG253-PRO276
B	ARG253-PRO276

site_id	SWS_FT_FI7
Number of Residues	64
Details	TRANSMEM: Helical; Name=5 => ECO:0000269\|PubMed:32433614, ECO:0000305\|PubMed:32433613, ECO:0007744\|PDB:6P2J, ECO:0007744\|PDB:6P2P, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	TRP320-ILE352
B	TRP320-ILE352

site_id	SWS_FT_FI8
Number of Residues	50
Details	TRANSMEM: Helical; Name=6 => ECO:0000269\|PubMed:32433614, ECO:0000305\|PubMed:32433613, ECO:0007744\|PDB:6P2J, ECO:0007744\|PDB:6P2P, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	ILE370-MET395
B	ILE370-MET395

site_id	SWS_FT_FI9
Number of Residues	48
Details	TRANSMEM: Helical; Name=7 => ECO:0000269\|PubMed:32433614, ECO:0000305\|PubMed:32433613, ECO:0007744\|PDB:6P2J, ECO:0007744\|PDB:6P2P, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	PHE444-LEU468
B	PHE444-LEU468

site_id	SWS_FT_FI10
Number of Residues	30
Details	TRANSMEM: Helical; Name=8 => ECO:0000269\|PubMed:32433614, ECO:0000305\|PubMed:32433613, ECO:0007744\|PDB:6P2J, ECO:0007744\|PDB:6P2P, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	LEU475-VAL490
B	LEU475-VAL490

site_id	SWS_FT_FI11
Number of Residues	62
Details	TRANSMEM: Helical; Name=9 => ECO:0000269\|PubMed:32433613, ECO:0000269\|PubMed:32433614, ECO:0007744\|PDB:6P2J, ECO:0007744\|PDB:6P2P, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	PRO497-CYS528
B	PRO497-CYS528

site_id	SWS_FT_FI12
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:16154994, ECO:0000269\|PubMed:16647063, ECO:0000269\|PubMed:32433613, ECO:0000269\|PubMed:32433614, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	HIS460
B	HIS460

site_id	SWS_FT_FI13
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:32433613, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	HIS137
A	ARG418
A	TYR433
A	SER456
B	HIS137
B	ARG418
B	TYR433
B	SER456

site_id	SWS_FT_FI14
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:32433614, ECO:0007744\|PDB:6P2P

Chain	Residue	Details
A	ASN415
B	ASN415

site_id	SWS_FT_FI15
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:32433614, ECO:0007744\|PDB:6P2J

Chain	Residue	Details
A	ASN421
B	ASN421

site_id	SWS_FT_FI16
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:32433613, ECO:0000269\|PubMed:32433614, ECO:0007744\|PDB:6P2J, ECO:0007744\|PDB:6P2P, ECO:0007744\|PDB:6VUM

Chain	Residue	Details
A	HIS425
A	LYS445
B	HIS425
B	LYS445

site_id	SWS_FT_FI17
Number of Residues	2
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	MET1
B	MET1

site_id	SWS_FT_FI18
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER8
B	SER8

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