Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5XK9

Crystal structure of Isosesquilavandulyl Diphosphate Synthase from Streptomyces sp. strain CNH-189 in complex with GSPP and DMAPP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016094	biological_process	polyprenol biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
A	0045547	molecular_function	ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
A	0046872	molecular_function	metal ion binding
B	0016094	biological_process	polyprenol biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
B	0045547	molecular_function	ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
B	0046872	molecular_function	metal ion binding
C	0016094	biological_process	polyprenol biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
C	0045547	molecular_function	ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
C	0046872	molecular_function	metal ion binding
D	0016094	biological_process	polyprenol biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
D	0045547	molecular_function	ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
D	0046872	molecular_function	metal ion binding
E	0016094	biological_process	polyprenol biosynthetic process
E	0016740	molecular_function	transferase activity
E	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
E	0045547	molecular_function	ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
E	0046872	molecular_function	metal ion binding
F	0016094	biological_process	polyprenol biosynthetic process
F	0016740	molecular_function	transferase activity
F	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
F	0045547	molecular_function	ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
F	0046872	molecular_function	metal ion binding
G	0016094	biological_process	polyprenol biosynthetic process
G	0016740	molecular_function	transferase activity
G	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
G	0045547	molecular_function	ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
G	0046872	molecular_function	metal ion binding
H	0016094	biological_process	polyprenol biosynthetic process
H	0016740	molecular_function	transferase activity
H	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
H	0045547	molecular_function	ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue MG A 500

Chain	Residue
A	ASP9
A	GST501
A	DMA502

site_id	AC2
Number of Residues	14
Details	binding site for residue GST A 501

Chain	Residue
A	TYR26
A	VAL52
A	TYR58
A	ARG60
A	ALA68
A	MET69
A	MG500
A	DMA502
A	PRO8
A	ASP9
A	GLY10
A	MET11
A	ARG12
A	ARG13

site_id	AC3
Number of Residues	14
Details	binding site for residue DMA A 502

Chain	Residue
A	LEU7
A	PRO8
A	ASP9
A	ASN57
A	ARG60
A	ARG163
A	ARG169
A	SER171
A	PHE173
A	MG500
A	GST501
A	HOH603
A	HOH623
A	HOH639

site_id	AC4
Number of Residues	6
Details	binding site for residue MG B 500

Chain	Residue
A	ARG211
A	HOH613
A	HOH626
B	ASP9
B	GST501
B	DMA502

site_id	AC5
Number of Residues	17
Details	binding site for residue GST B 501

Chain	Residue
A	ARG211
A	HOH613
A	HOH626
B	PRO8
B	ASP9
B	GLY10
B	MET11
B	ARG12
B	ARG13
B	TYR26
B	VAL52
B	ASN57
B	ARG60
B	ALA68
B	PHE72
B	MG500
B	DMA502

site_id	AC6
Number of Residues	20
Details	binding site for residue DMA B 502

Chain	Residue
A	PHE180
A	ARG211
A	TYR212
A	GLY213
A	HOH613
B	LEU7
B	PRO8
B	ASP9
B	THR51
B	VAL52
B	ASN57
B	ARG163
B	ARG169
B	SER171
B	PHE173
B	MG500
B	GST501
B	HOH601
B	HOH609
B	HOH655

site_id	AC7
Number of Residues	5
Details	binding site for residue MG C 500

Chain	Residue
C	ASP9
C	HIS167
C	GST501
C	DMA502
C	HOH702

site_id	AC8
Number of Residues	15
Details	binding site for residue GST C 501

Chain	Residue
C	PRO8
C	ASP9
C	GLY10
C	MET11
C	ARG12
C	ARG13
C	TYR26
C	VAL52
C	SER53
C	ASN57
C	ARG60
C	ALA68
C	MG500
C	DMA502
C	HOH624

site_id	AC9
Number of Residues	12
Details	binding site for residue DMA C 502

Chain	Residue
C	ARG163
C	ARG169
C	SER171
C	PHE173
C	MG500
C	GST501
C	HOH670
C	LEU7
C	PRO8
C	ARG12
C	SER54
C	ASN57

site_id	AD1
Number of Residues	5
Details	binding site for residue MG D 500

Chain	Residue
D	ASP9
D	GST501
D	DMA502
D	HOH602
D	HOH609

site_id	AD2
Number of Residues	18
Details	binding site for residue GST D 501

Chain	Residue
C	ARG211
C	TYR215
D	PRO8
D	ASP9
D	GLY10
D	MET11
D	ARG12
D	ARG13
D	TYR26
D	VAL52
D	ASN57
D	TYR58
D	ARG60
D	ALA68
D	PHE72
D	MG500
D	DMA502
D	HOH609

site_id	AD3
Number of Residues	19
Details	binding site for residue DMA D 502

Chain	Residue
C	ARG211
C	TYR212
C	GLY213
D	PRO8
D	ASP9
D	THR51
D	VAL52
D	ASN57
D	ARG60
D	ARG163
D	ARG169
D	SER171
D	PHE173
D	MG500
D	GST501
D	HOH602
D	HOH603
D	HOH611
D	HOH630

site_id	AD4
Number of Residues	4
Details	binding site for residue MG E 500

Chain	Residue
E	ASP9
E	GST501
E	DMA502
E	HOH662

site_id	AD5
Number of Residues	14
Details	binding site for residue GST E 501

Chain	Residue
E	PRO8
E	ASP9
E	GLY10
E	MET11
E	ARG12
E	ARG13
E	VAL52
E	TYR58
E	ARG60
E	ALA68
E	MET69
E	PHE72
E	MG500
E	DMA502

site_id	AD6
Number of Residues	15
Details	binding site for residue DMA E 502

Chain	Residue
E	LEU7
E	PRO8
E	ASP9
E	ASN57
E	ARG60
E	ARG163
E	ARG169
E	SER171
E	PHE173
E	MG500
E	GST501
E	HOH601
E	HOH602
E	HOH605
E	HOH614

site_id	AD7
Number of Residues	6
Details	binding site for residue MG F 500

Chain	Residue
E	ARG211
F	ASP9
F	GST501
F	DMA502
F	HOH610
F	HOH619

site_id	AD8
Number of Residues	16
Details	binding site for residue GST F 501

Chain	Residue
E	ARG211
F	PRO8
F	ASP9
F	GLY10
F	MET11
F	ARG12
F	ARG13
F	TYR26
F	ASN57
F	ARG60
F	ALA68
F	PHE72
F	MG500
F	DMA502
F	HOH610
F	HOH624

site_id	AD9
Number of Residues	19
Details	binding site for residue DMA F 502

Chain	Residue
E	TYR212
E	GLY213
F	PRO8
F	ASP9
F	THR51
F	VAL52
F	SER53
F	ASN57
F	ARG163
F	ARG169
F	SER171
F	PHE173
F	MG500
F	GST501
F	HOH602
F	HOH610
F	HOH614
F	HOH619
F	HOH634

site_id	AE1
Number of Residues	4
Details	binding site for residue MG G 500

Chain	Residue
G	ASP9
G	GST501
G	DMA502
G	HOH652

site_id	AE2
Number of Residues	15
Details	binding site for residue GST G 501

Chain	Residue
G	PRO8
G	ASP9
G	GLY10
G	MET11
G	ARG12
G	ARG13
G	TYR26
G	SER53
G	ASN57
G	ARG60
G	ALA68
G	MG500
G	DMA502
G	HOH623
G	HOH652

site_id	AE3
Number of Residues	13
Details	binding site for residue DMA G 502

Chain	Residue
G	LEU7
G	PRO8
G	ARG12
G	SER54
G	ASN57
G	ARG60
G	ARG163
G	ARG169
G	SER171
G	PHE173
G	MG500
G	GST501
G	HOH672

site_id	AE4
Number of Residues	6
Details	binding site for residue MG H 500

Chain	Residue
G	ARG211
H	ASP9
H	GST501
H	DMA502
H	HOH613
H	HOH624

site_id	AE5
Number of Residues	19
Details	binding site for residue GST H 501

Chain	Residue
G	ARG211
G	TYR215
H	PRO8
H	ASP9
H	GLY10
H	MET11
H	ARG12
H	ARG13
H	TYR26
H	VAL52
H	ASN57
H	TYR58
H	ARG60
H	ALA68
H	PHE72
H	MG500
H	DMA502
H	HOH613
H	HOH624

site_id	AE6
Number of Residues	19
Details	binding site for residue DMA H 502

Chain	Residue
G	ARG211
G	TYR212
G	GLY213
H	PRO8
H	ASP9
H	THR51
H	VAL52
H	ASN57
H	ARG60
H	ARG163
H	ARG169
H	SER171
H	PHE173
H	MG500
H	GST501
H	HOH607
H	HOH611
H	HOH613
H	HOH621

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