Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3PDE

Crystal structure of geranylgeranyl pyrophosphate synthase from Lactobacillus brevis atcc 367 complexed with isoprenyl diphosphate and magnesium

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004337	molecular_function	(2E,6E)-farnesyl diphosphate synthase activity
A	0004659	molecular_function	prenyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0008299	biological_process	isoprenoid biosynthetic process
A	0016114	biological_process	terpenoid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0045337	biological_process	farnesyl diphosphate biosynthetic process
A	0046872	molecular_function	metal ion binding
B	0004337	molecular_function	(2E,6E)-farnesyl diphosphate synthase activity
B	0004659	molecular_function	prenyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0008299	biological_process	isoprenoid biosynthetic process
B	0016114	biological_process	terpenoid biosynthetic process
B	0016740	molecular_function	transferase activity
B	0045337	biological_process	farnesyl diphosphate biosynthetic process
B	0046872	molecular_function	metal ion binding
C	0004337	molecular_function	(2E,6E)-farnesyl diphosphate synthase activity
C	0004659	molecular_function	prenyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0008299	biological_process	isoprenoid biosynthetic process
C	0016114	biological_process	terpenoid biosynthetic process
C	0016740	molecular_function	transferase activity
C	0045337	biological_process	farnesyl diphosphate biosynthetic process
C	0046872	molecular_function	metal ion binding
D	0004337	molecular_function	(2E,6E)-farnesyl diphosphate synthase activity
D	0004659	molecular_function	prenyltransferase activity
D	0005737	cellular_component	cytoplasm
D	0008299	biological_process	isoprenoid biosynthetic process
D	0016114	biological_process	terpenoid biosynthetic process
D	0016740	molecular_function	transferase activity
D	0045337	biological_process	farnesyl diphosphate biosynthetic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE DMA A 309

Chain	Residue
A	GLY47
A	HOH333
A	HOH353
A	HOH661
A	HOH699
A	HOH879
A	HOH978
A	LYS48
A	ARG51
A	HIS82
A	LEU86
A	ARG101
A	THR184
A	PHE220
A	DMA310

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DMA A 310

Chain	Residue
A	SER85
A	ASP89
A	ASP95
A	ARG100
A	LYS183
A	DMA309
A	MG311
A	MG312
A	HOH852
A	HOH878
A	HOH966
A	HOH970

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 311

Chain	Residue
A	ASP89
A	ASP95
A	DMA310
A	MG312
A	HOH584
A	HOH965
A	HOH971

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 312

Chain	Residue
A	ASP89
A	ASP95
A	DMA310
A	MG311
A	HOH878
A	HOH970

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 313

Chain	Residue
A	LEU275
A	LEU278
A	PRO279
A	THR280
A	SER281
A	ARG284
A	ASP285
A	HOH481

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DMA B 309

Chain	Residue
B	GLY47
B	LYS48
B	ARG51
B	HIS82
B	ARG101
B	PHE220
B	DMA312
B	HOH338
B	HOH422
B	HOH791
B	HOH794
B	HOH921
B	HOH985

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG B 310

Chain	Residue
B	ASP89
B	ASP95
B	ASP163
B	MG311
B	DMA312
B	HOH636
B	HOH973

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 311

Chain	Residue
B	ASP89
B	ASP95
B	MG310
B	DMA312
B	HOH617
B	HOH828

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DMA B 312

Chain	Residue
B	SER85
B	LEU86
B	ASP89
B	ASP95
B	ARG100
B	MET156
B	GLN160
B	LYS183
B	DMA309
B	MG310
B	MG311
B	HOH617
B	HOH828
B	HOH974
B	HOH1041
B	HOH1126

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE DMA C 309

Chain	Residue
C	HOH339
C	HOH382
C	HOH604
C	HOH717
C	HOH987
C	HOH994
C	GLY47
C	LYS48
C	ARG51
C	HIS82
C	LEU86
C	ARG101
C	THR184
C	PHE220
C	DMA310

site_id	BC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE DMA C 310

Chain	Residue
C	SER85
C	ASP89
C	ASP95
C	ARG100
C	MET156
C	GLN160
C	LYS183
C	DMA309
C	MG311
C	MG312
C	HOH596
C	HOH795
C	HOH800
C	HOH847
C	HOH995

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 311

Chain	Residue
C	ASP89
C	ASP95
C	DMA310
C	MG312
C	HOH795
C	HOH800

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG C 312

Chain	Residue
C	ASP89
C	ASP95
C	ASP163
C	DMA310
C	MG311
C	HOH596
C	HOH989

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 313

Chain	Residue
C	PRO21
C	PRO68
C	ARG73
C	GLN175
C	HOH345
C	HOH371

site_id	BC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DMA D 309

Chain	Residue
D	GLY47
D	LYS48
D	ARG51
D	HIS82
D	ARG101
D	PHE220
D	DMA312
D	HOH342
D	HOH585
D	HOH597
D	HOH938
D	HOH944
D	HOH956

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 310

Chain	Residue
D	ASP89
D	ASP95
D	MG311
D	DMA312
D	HOH434
D	HOH958

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG D 311

Chain	Residue
D	ASP89
D	ASP95
D	MG310
D	DMA312
D	HOH753
D	HOH822
D	HOH957

site_id	BC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DMA D 312

Chain	Residue
D	SER85
D	ASP89
D	ASP95
D	ARG100
D	LYS183
D	DMA309
D	MG310
D	MG311
D	HOH434
D	HOH889
D	HOH932
D	HOH957
D	HOH958
D	HOH1081

Functional Information from PROSITE/UniProt

site_id	PS00444
Number of Residues	13
Details	POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. FGlaFQIyDDIlD

Chain	Residue	Details
A	PHE216-ASP228

site_id	PS00723
Number of Residues	17
Details	POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LIhDDlpamDndalRRG

Chain	Residue	Details
A	LEU86-GLY102

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