Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3LEE

Crystal structure of the human squalene synthase complexed with BPH-652

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	10
Details	BINDING SITE FOR RESIDUE B65 A 451

Chain	Residue
A	HOH1
A	MG452
A	TYR73
A	ARG77
A	ASP80
A	GLU83
A	ASP84
A	VAL175
A	VAL179
A	GLN212

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 452

Chain	Residue
A	ASP80
A	GLU83
A	ASP84
A	B65451

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE B65 B 451

Chain	Residue
B	HOH5
B	PHE54
B	TYR73
B	ARG77
B	ASP80
B	ASP84
B	VAL175
B	VAL179
B	MG452

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 452

Chain	Residue
B	ASP80
B	GLU83
B	ASP84
B	B65451

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE B65 C 451

Chain	Residue
C	PHE54
C	TYR73
C	ARG77
C	ASP80
C	ASP84
C	VAL175
C	HOH380
C	MG452

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 452

Chain	Residue
C	ASP80
C	GLU83
C	ASP84
C	B65451

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE B65 D 451

Chain	Residue
D	TYR73
D	LEU76
D	ARG77
D	ASP80
D	GLU83
D	ASP84
D	VAL175
D	VAL179
D	MG452

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 452

Chain	Residue
D	ASP80
D	ASP84
D	HOH395
D	B65451

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE B65 E 451

Chain	Residue
E	PHE54
E	TYR73
E	ASP80
E	GLU83
E	ASP84
E	VAL175
E	VAL179
E	GLN212
E	ARG228
E	HOH372
E	MG452

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 452

Chain	Residue
E	GLU83
E	TYR171
E	VAL175
E	B65451

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE B65 F 451

Chain	Residue
F	PHE54
F	LEU76
F	ARG77
F	ASP80
F	VAL179
F	GLN212
F	HOH377
F	MG452

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 452

Chain	Residue
F	ASP80
F	GLU83
F	ASP84
F	B65451

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	100
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	22
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	2
Details	M-CSA 264

Chain	Residue	Details
F	TYR171	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
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)