Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3VJC

Crystal structure of the human squalene synthase in complex with zaragozic acid A

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	21
Details	BINDING SITE FOR RESIDUE ZGA A 400

Chain	Residue
A	THR50
A	VAL175
A	ALA296
A	HOH474
A	HOH475
A	HOH501
A	HOH932
A	HOH935
A	HOH1109
A	HOH1110
A	HOH1797
A	SER51
A	HOH1825
B	VAL322
A	ARG52
A	SER53
A	PHE54
A	TYR73
A	ARG77
A	ASP80
A	LYS117

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 401

Chain	Residue
A	ARG149
A	HIS173
A	TYR174
A	HOH545
A	HOH547
A	HOH1173
A	HOH1785
A	HOH1788

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ZGA B 400

Chain	Residue
B	THR50
B	SER51
B	ARG52
B	SER53
B	PHE54
B	TYR73
B	ARG77
B	ASP80
B	LYS117
B	MET150
B	VAL175
B	VAL179
B	ASN215
B	ARG218
B	HOH692
B	HOH999
B	HOH1323
B	HOH1633
B	HOH1670

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B 401

Chain	Residue
B	ARG149
B	HIS173
B	TYR174
B	HOH721
B	HOH722
B	HOH723
B	HOH724
B	HOH1385
B	HOH1816

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG B 402

Chain	Residue
B	GLU191

site_id	AC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ZGA C 400

Chain	Residue
C	THR50
C	SER51
C	ARG52
C	SER53
C	PHE54
C	TYR73
C	ARG77
C	ASP80
C	LYS117
C	MET150
C	VAL175
C	VAL179
C	LEU211
C	THR214
C	ASN215
C	ARG218
C	PRO292
C	ALA296
C	THR299
C	HOH786
C	HOH787
C	HOH1029
C	HOH1429
C	HOH1431
C	HOH1698
C	HOH1708

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 C 401

Chain	Residue
C	ARG149
C	HIS173
C	TYR174
C	HOH825
C	HOH826
C	HOH837
C	HOH1482
C	HOH1483
C	HOH1790

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ZGA D 400

Chain	Residue
D	ARG77
D	ASP80
D	LYS117
D	MET150
D	VAL175
D	VAL179
D	LEU211
D	THR214
D	ASN215
D	ARG218
D	PRO292
D	MET295
D	HOH1531
D	HOH1534
D	HOH1692
D	THR50
D	SER51
D	ARG52
D	SER53
D	PHE54
D	TYR73

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 401

Chain	Residue
D	ARG149
D	HIS173
D	TYR174
D	HOH1551
D	HOH1637
D	HOH1672

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG D 402

Chain	Residue
D	GLU191

site_id	BC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ZGA E 400

Chain	Residue
E	THR50
E	SER51
E	ARG52
E	SER53
E	PHE54
E	TYR73
E	ARG77
E	MET150
E	VAL175
E	VAL179
E	ASN215
E	ARG218
E	ALA296
E	HOH903
E	HOH1602
E	HOH1603

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 E 401

Chain	Residue
E	ARG149
E	HIS173
E	TYR174
E	HOH1082
E	HOH1366
E	HOH1367
E	HOH1368
E	HOH1777

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ZGA F 400

Chain	Residue
F	THR50
F	SER51
F	ARG52
F	SER53
F	PHE54
F	TYR73
F	ARG77
F	VAL175
F	LEU211
F	ASN215
F	ARG218
F	THR299
F	HOH1744
F	HOH1766

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 F 401

Chain	Residue
F	ARG149
F	HIS173
F	TYR174
F	HOH1621

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	30
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)