Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2Q80

Crystal structure of human geranylgeranyl pyrophosphate synthase bound to GGPP

Replaces: 2FVI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004161	molecular_function	dimethylallyltranstransferase activity
A	0004311	molecular_function	farnesyltranstransferase activity
A	0004337	molecular_function	geranyltranstransferase activity
A	0004659	molecular_function	prenyltransferase activity
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006720	biological_process	isoprenoid metabolic process
A	0008299	biological_process	isoprenoid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030018	cellular_component	Z disc
A	0033384	biological_process	geranyl diphosphate biosynthetic process
A	0033386	biological_process	geranylgeranyl diphosphate biosynthetic process
A	0042802	molecular_function	identical protein binding
A	0045337	biological_process	farnesyl diphosphate biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0048471	cellular_component	perinuclear region of cytoplasm
B	0004161	molecular_function	dimethylallyltranstransferase activity
B	0004311	molecular_function	farnesyltranstransferase activity
B	0004337	molecular_function	geranyltranstransferase activity
B	0004659	molecular_function	prenyltransferase activity
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006720	biological_process	isoprenoid metabolic process
B	0008299	biological_process	isoprenoid biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030018	cellular_component	Z disc
B	0033384	biological_process	geranyl diphosphate biosynthetic process
B	0033386	biological_process	geranylgeranyl diphosphate biosynthetic process
B	0042802	molecular_function	identical protein binding
B	0045337	biological_process	farnesyl diphosphate biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0048471	cellular_component	perinuclear region of cytoplasm
C	0004161	molecular_function	dimethylallyltranstransferase activity
C	0004311	molecular_function	farnesyltranstransferase activity
C	0004337	molecular_function	geranyltranstransferase activity
C	0004659	molecular_function	prenyltransferase activity
C	0005515	molecular_function	protein binding
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006720	biological_process	isoprenoid metabolic process
C	0008299	biological_process	isoprenoid biosynthetic process
C	0016740	molecular_function	transferase activity
C	0030018	cellular_component	Z disc
C	0033384	biological_process	geranyl diphosphate biosynthetic process
C	0033386	biological_process	geranylgeranyl diphosphate biosynthetic process
C	0042802	molecular_function	identical protein binding
C	0045337	biological_process	farnesyl diphosphate biosynthetic process
C	0046872	molecular_function	metal ion binding
C	0048471	cellular_component	perinuclear region of cytoplasm
D	0004161	molecular_function	dimethylallyltranstransferase activity
D	0004311	molecular_function	farnesyltranstransferase activity
D	0004337	molecular_function	geranyltranstransferase activity
D	0004659	molecular_function	prenyltransferase activity
D	0005515	molecular_function	protein binding
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006720	biological_process	isoprenoid metabolic process
D	0008299	biological_process	isoprenoid biosynthetic process
D	0016740	molecular_function	transferase activity
D	0030018	cellular_component	Z disc
D	0033384	biological_process	geranyl diphosphate biosynthetic process
D	0033386	biological_process	geranylgeranyl diphosphate biosynthetic process
D	0042802	molecular_function	identical protein binding
D	0045337	biological_process	farnesyl diphosphate biosynthetic process
D	0046872	molecular_function	metal ion binding
D	0048471	cellular_component	perinuclear region of cytoplasm
E	0004161	molecular_function	dimethylallyltranstransferase activity
E	0004311	molecular_function	farnesyltranstransferase activity
E	0004337	molecular_function	geranyltranstransferase activity
E	0004659	molecular_function	prenyltransferase activity
E	0005515	molecular_function	protein binding
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006720	biological_process	isoprenoid metabolic process
E	0008299	biological_process	isoprenoid biosynthetic process
E	0016740	molecular_function	transferase activity
E	0030018	cellular_component	Z disc
E	0033384	biological_process	geranyl diphosphate biosynthetic process
E	0033386	biological_process	geranylgeranyl diphosphate biosynthetic process
E	0042802	molecular_function	identical protein binding
E	0045337	biological_process	farnesyl diphosphate biosynthetic process
E	0046872	molecular_function	metal ion binding
E	0048471	cellular_component	perinuclear region of cytoplasm
F	0004161	molecular_function	dimethylallyltranstransferase activity
F	0004311	molecular_function	farnesyltranstransferase activity
F	0004337	molecular_function	geranyltranstransferase activity
F	0004659	molecular_function	prenyltransferase activity
F	0005515	molecular_function	protein binding
F	0005654	cellular_component	nucleoplasm
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006720	biological_process	isoprenoid metabolic process
F	0008299	biological_process	isoprenoid biosynthetic process
F	0016740	molecular_function	transferase activity
F	0030018	cellular_component	Z disc
F	0033384	biological_process	geranyl diphosphate biosynthetic process
F	0033386	biological_process	geranylgeranyl diphosphate biosynthetic process
F	0042802	molecular_function	identical protein binding
F	0045337	biological_process	farnesyl diphosphate biosynthetic process
F	0046872	molecular_function	metal ion binding
F	0048471	cellular_component	perinuclear region of cytoplasm

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 400

Chain	Residue
A	ASP64
A	ASP68
A	GLN126
A	MG401
A	GRG500

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	GRG500
A	ASP64
A	ASP68
A	LYS202
A	MG400

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 400

Chain	Residue
B	ASP64
B	ASP68
B	GLN126
B	ASP129
B	MG401
B	GRG500

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 401

Chain	Residue
B	ASP64
B	ASP68
B	GLU210
B	MG400
B	GRG500

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 400

Chain	Residue
C	ASP64
C	ASP68
C	GLN126
C	ASP129
C	GRG500

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 401

Chain	Residue
C	ASP64
C	ASP68
C	GRG500

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 400

Chain	Residue
D	ASP64
D	ASP68
D	GLN126
D	ASP129
D	GRG500

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 401

Chain	Residue
D	ASP64
D	ASP68
D	GRG500

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 400

Chain	Residue
E	ASP64
E	ASP68
E	MG401
E	GRG500

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 401

Chain	Residue
E	ASP64
E	ASP68
E	MG400
E	GRG500

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 400

Chain	Residue
F	ASP64
F	ASP68
F	GLN126
F	ASP129
F	MG401
F	GRG500

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 401

Chain	Residue
F	ASP64
F	ASP68
F	MG400
F	GRG500

site_id	BC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GRG A 500

Chain	Residue
A	LEU31
A	SER32
A	THR53
A	ASP64
A	ASP68
A	ARG73
A	GLN126
A	LYS151
A	LEU155
A	PHE156
A	ALA159
A	VAL160
A	GLN185
A	ASP188
A	LYS202
A	LYS212
A	MG400
A	MG401

site_id	BC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GRG B 500

Chain	Residue
B	SER32
B	THR53
B	SER60
B	ASP64
B	ASP68
B	ARG73
B	GLN126
B	LYS151
B	ALA159
B	GLN185
B	LYS202
B	LYS212
B	MG400
B	MG401

site_id	BC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GRG C 500

Chain	Residue
C	GLN185
C	ASP188
C	LYS212
C	MG400
C	MG401
C	ARG28
C	SER32
C	THR53
C	HIS57
C	ASP64
C	ASP68
C	ARG73
C	GLN126
C	LYS151
C	PHE156
C	ALA159
C	MET163

site_id	BC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE GRG D 500

Chain	Residue
D	SER32
D	THR53
D	ASP64
D	ASP68
D	ARG73
D	GLN126
D	LYS151
D	PHE156
D	ALA159
D	VAL160
D	GLN185
D	ASP188
D	LYS202
D	LYS212
D	MG400
D	MG401

site_id	BC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GRG E 500

Chain	Residue
E	LEU31
E	SER32
E	PHE35
E	THR53
E	ASP64
E	ASP68
E	ARG73
E	LYS151
E	ALA159
E	GLN185
E	ASP188
E	LYS202
E	LYS212
E	MG400
E	MG401

site_id	BC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GRG F 500

Chain	Residue
F	ASP64
F	ASP68
F	ARG73
F	GLN126
F	LYS151
F	LEU155
F	GLN185
F	ASP188
F	LYS202
F	MG400
F	MG401

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU180-ASN192

site_id	PS00723
Number of Residues	15
Details	POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LLiDDie..DnsklRRG

Chain	Residue	Details
A	LEU61-GLY75

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P14324

Chain	Residue	Details
A	LYS25
D	LYS25
D	ARG28
D	ARG74
E	LYS25
E	ARG28
E	ARG74
F	LYS25
F	ARG28
F	ARG74
A	ARG28
A	ARG74
B	LYS25
B	ARG28
B	ARG74
C	LYS25
C	ARG28
C	ARG74

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q12051

Chain	Residue	Details
A	HIS57
B	HIS57
C	HIS57
D	HIS57
E	HIS57
F	HIS57

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:16698791

Chain	Residue	Details
A	ASP64
E	ASP68
F	ASP64
F	ASP68
A	ASP68
B	ASP64
B	ASP68
C	ASP64
C	ASP68
D	ASP64
D	ASP68
E	ASP64

site_id	SWS_FT_FI4
Number of Residues	30
Details	BINDING:

Chain	Residue	Details
A	ARG73
B	LYS202
C	ARG73
C	LYS151
C	THR152
C	GLN185
C	LYS202
D	ARG73
D	LYS151
D	THR152
D	GLN185
A	LYS151
D	LYS202
E	ARG73
E	LYS151
E	THR152
E	GLN185
E	LYS202
F	ARG73
F	LYS151
F	THR152
F	GLN185
A	THR152
F	LYS202
A	GLN185
A	LYS202
B	ARG73
B	LYS151
B	THR152
B	GLN185

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	LYS212
B	LYS212
C	LYS212
D	LYS212
E	LYS212
F	LYS212

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	MET1
B	MET1
C	MET1
D	MET1
E	MET1
F	MET1

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1fps

Chain	Residue	Details
A	ARG73
A	PHE184

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1fps

Chain	Residue	Details
B	ARG73
B	PHE184

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1fps

Chain	Residue	Details
C	ARG73
C	PHE184

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1fps

Chain	Residue	Details
D	ARG73
D	PHE184

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1fps

Chain	Residue	Details
E	ARG73
E	PHE184

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1fps

Chain	Residue	Details
F	ARG73
F	PHE184

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