Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3WEF

Crystal structure of the human squalene synthase in complex with farnesyl thiopyrophosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008610	biological_process	lipid biosynthetic process
A	0009058	biological_process	biosynthetic process
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
A	0045338	biological_process	farnesyl diphosphate metabolic process
A	0051996	molecular_function	squalene synthase [NAD(P)H] activity
B	0008610	biological_process	lipid biosynthetic process
B	0009058	biological_process	biosynthetic process
B	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
B	0045338	biological_process	farnesyl diphosphate metabolic process
B	0051996	molecular_function	squalene synthase [NAD(P)H] activity
C	0008610	biological_process	lipid biosynthetic process
C	0009058	biological_process	biosynthetic process
C	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
C	0045338	biological_process	farnesyl diphosphate metabolic process
C	0051996	molecular_function	squalene synthase [NAD(P)H] activity
D	0008610	biological_process	lipid biosynthetic process
D	0009058	biological_process	biosynthetic process
D	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
D	0045338	biological_process	farnesyl diphosphate metabolic process
D	0051996	molecular_function	squalene synthase [NAD(P)H] activity
E	0008610	biological_process	lipid biosynthetic process
E	0009058	biological_process	biosynthetic process
E	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
E	0045338	biological_process	farnesyl diphosphate metabolic process
E	0051996	molecular_function	squalene synthase [NAD(P)H] activity
F	0008610	biological_process	lipid biosynthetic process
F	0009058	biological_process	biosynthetic process
F	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
F	0045338	biological_process	farnesyl diphosphate metabolic process
F	0051996	molecular_function	squalene synthase [NAD(P)H] activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE FPS A 401

Chain	Residue
A	THR50
A	GLN212
A	ASN215
A	CYS289
A	FPS402
A	SER51
A	ARG52
A	SER53
A	PHE54
A	ARG77
A	GLY180
A	MET207
A	LEU211

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FPS A 402

Chain	Residue
A	ILE58
A	TYR73
A	ARG77
A	ASP80
A	ASP84
A	VAL175
A	PHE288
A	FPS401

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE FPS B 401

Chain	Residue
B	THR50
B	ARG52
B	SER53
B	PHE54
B	TYR73
B	ARG77
B	VAL179
B	GLY180
B	MET207
B	LEU211
B	GLN212
B	TYR276
B	CYS289
B	FPS402

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE FPS B 402

Chain	Residue
B	TYR73
B	ARG77
B	ASP80
B	GLU83
B	ASP84
B	MET150
B	MET154
B	TYR171
B	VAL175
B	VAL179
B	GLN212
B	PHE288
B	FPS401

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE FPS C 401

Chain	Residue
C	THR50
C	SER51
C	ARG52
C	SER53
C	PHE54
C	ARG77
C	GLY180
C	MET207
C	LEU211
C	GLN212
C	ASN215
C	CYS289

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE FPS D 401

Chain	Residue
D	THR50
D	SER51
D	SER53
D	PHE54
D	TYR73
D	ARG77
D	GLY180
D	LEU183
D	MET207
D	GLN212
D	ASN215
D	PHE288
D	CYS289
D	HOH505
D	HOH516
D	HOH520

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE FPS E 401

Chain	Residue
E	THR50
E	SER51
E	ARG52
E	SER53
E	PHE54
E	TYR73
E	GLY180
E	MET207
E	LEU211
E	GLN212
E	ASN215
E	CYS289
E	FPS402

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FPS E 402

Chain	Residue
E	FPS401
E	TYR73
E	ARG77
E	ASP80
E	GLU83
E	ASP84
E	TYR171
E	VAL175
E	GLN212
E	ARG228
E	PHE230

Functional Information from PROSITE/UniProt

site_id	PS01044
Number of Residues	16
Details	SQUALEN_PHYTOEN_SYN_1 Squalene and phytoene synthases signature 1. YChyVAGLVGigLsrL

Chain	Residue	Details
A	TYR171-LEU186

site_id	PS01045
Number of Residues	26
Details	SQUALEN_PHYTOEN_SYN_2 Squalene and phytoene synthases signature 2. MGlflQkt.NIiRDYleDqqgg...ReFwP

Chain	Residue	Details
A	MET207-PRO232

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	120
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	27
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24531458","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24531458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3WEG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WEH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 264

Chain	Residue	Details
A	TYR171	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ARG218	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
A	ARG228	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
A	PHE288	polar/non-polar interaction, steric role, van der waals interaction

site_id	MCSA2
Number of Residues	4
Details	M-CSA 264

Chain	Residue	Details
B	TYR171	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ARG218	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
B	ARG228	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
B	PHE288	polar/non-polar interaction, steric role, van der waals interaction

site_id	MCSA3
Number of Residues	4
Details	M-CSA 264

Chain	Residue	Details
C	TYR171	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ARG218	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
C	ARG228	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
C	PHE288	polar/non-polar interaction, steric role, van der waals interaction

site_id	MCSA4
Number of Residues	4
Details	M-CSA 264

Chain	Residue	Details
D	TYR171	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ARG218	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
D	ARG228	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
D	PHE288	polar/non-polar interaction, steric role, van der waals interaction

site_id	MCSA5
Number of Residues	4
Details	M-CSA 264

Chain	Residue	Details
E	TYR171	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	ARG218	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
E	ARG228	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
E	PHE288	polar/non-polar interaction, steric role, van der waals interaction

site_id	MCSA6
Number of Residues	4
Details	M-CSA 264

Chain	Residue	Details
F	TYR171	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	ARG218	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
F	ARG228	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
F	PHE288	polar/non-polar interaction, steric role, van der waals interaction

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)