4KPJ

Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant complexed with Mg, Pamidronate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004659	molecular_function	prenyltransferase activity
A	0008299	biological_process	isoprenoid biosynthetic process
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE 210 A 901

Chain	Residue
A	LEU100
A	MG902
A	MG903
A	MG904
A	EDO906
A	HOH1001
A	HOH1002
A	HOH1004
A	HOH1005
A	HOH1006
A	HOH1007
A	ASP103
A	HOH1008
A	HOH1009
A	HOH1015
A	HOH1017
A	HOH1153
A	HOH1221
A	ASP107
A	ARG112
A	LYS200
A	THR201
A	GLN240
A	ASP243
A	LYS257

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 902

Chain	Residue
A	ASP103
A	ASP107
A	210901
A	MG904
A	HOH1004
A	HOH1005

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 903

Chain	Residue
A	ASP243
A	210901
A	HOH1006
A	HOH1007
A	HOH1008

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 904

Chain	Residue
A	ASP103
A	ASP107
A	210901
A	MG902
A	HOH1001
A	HOH1002
A	HOH1003

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 905

Chain	Residue
A	LEU248
A	ILE262
A	SER268
A	LEU270
A	VAL271
A	TYR290
A	TYR305
A	HOH1080
A	HOH1081

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 906

Chain	Residue
A	GLN96
A	LYS200
A	THR201
A	ALA204
A	SER205
A	210901

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 907

Chain	Residue
A	PRO151
A	TYR152
A	LEU154
A	ASN155

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 908

Chain	Residue
A	LEU246
A	ASP247
A	GLY250
A	PRO252
A	THR255
A	LYS257
A	GLY259
A	HOH1244

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 909

Chain	Residue
A	ALA299
A	HIS324
A	HOH1195
A	HOH1258

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 910

Chain	Residue
A	GLN282
A	ILE285
A	ARG300
A	GLU307
A	HOH1171

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	MET235-ASP247

---

site_id	PS00723
Number of Residues	15
Details	POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVaDDim..DssltRRG

Chain	Residue	Details
A	LEU100-GLY114

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16684881","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZW5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Important for determining product chain length","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---