Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5YGK

Crystal structure of a synthase from Streptomyces sp. CL190 with dmaspp

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002094	molecular_function	polyprenyltransferase activity
A	0005886	cellular_component	plasma membrane
A	0009409	biological_process	response to cold
A	0009668	biological_process	plastid membrane organization
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	0033850	molecular_function	Z-farnesyl diphosphate synthase activity
A	0045547	molecular_function	dehydrodolichyl diphosphate synthase activity
A	0046872	molecular_function	metal ion binding
B	0002094	molecular_function	polyprenyltransferase activity
B	0005886	cellular_component	plasma membrane
B	0009409	biological_process	response to cold
B	0009668	biological_process	plastid membrane organization
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	0033850	molecular_function	Z-farnesyl diphosphate synthase activity
B	0045547	molecular_function	dehydrodolichyl diphosphate synthase activity
B	0046872	molecular_function	metal ion binding
C	0002094	molecular_function	polyprenyltransferase activity
C	0005886	cellular_component	plasma membrane
C	0009409	biological_process	response to cold
C	0009668	biological_process	plastid membrane organization
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	0033850	molecular_function	Z-farnesyl diphosphate synthase activity
C	0045547	molecular_function	dehydrodolichyl diphosphate synthase activity
C	0046872	molecular_function	metal ion binding
D	0002094	molecular_function	polyprenyltransferase activity
D	0005886	cellular_component	plasma membrane
D	0009409	biological_process	response to cold
D	0009668	biological_process	plastid membrane organization
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	0033850	molecular_function	Z-farnesyl diphosphate synthase activity
D	0045547	molecular_function	dehydrodolichyl diphosphate synthase activity
D	0046872	molecular_function	metal ion binding
E	0002094	molecular_function	polyprenyltransferase activity
E	0005886	cellular_component	plasma membrane
E	0009409	biological_process	response to cold
E	0009668	biological_process	plastid membrane organization
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	0033850	molecular_function	Z-farnesyl diphosphate synthase activity
E	0045547	molecular_function	dehydrodolichyl diphosphate synthase activity
E	0046872	molecular_function	metal ion binding
F	0002094	molecular_function	polyprenyltransferase activity
F	0005886	cellular_component	plasma membrane
F	0009409	biological_process	response to cold
F	0009668	biological_process	plastid membrane organization
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	0033850	molecular_function	Z-farnesyl diphosphate synthase activity
F	0045547	molecular_function	dehydrodolichyl diphosphate synthase activity
F	0046872	molecular_function	metal ion binding
G	0002094	molecular_function	polyprenyltransferase activity
G	0005886	cellular_component	plasma membrane
G	0009409	biological_process	response to cold
G	0009668	biological_process	plastid membrane organization
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	0033850	molecular_function	Z-farnesyl diphosphate synthase activity
G	0045547	molecular_function	dehydrodolichyl diphosphate synthase activity
G	0046872	molecular_function	metal ion binding
H	0002094	molecular_function	polyprenyltransferase activity
H	0005886	cellular_component	plasma membrane
H	0009409	biological_process	response to cold
H	0009668	biological_process	plastid membrane organization
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	0033850	molecular_function	Z-farnesyl diphosphate synthase activity
H	0045547	molecular_function	dehydrodolichyl diphosphate synthase activity
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue DST A 301

Chain	Residue
A	LEU7
A	MG303
A	HOH423
A	HOH460
A	PRO8
A	ASP9
A	THR51
A	ARG163
A	ARG169
A	SER171
A	PHE173
A	DST302

site_id	AC2
Number of Residues	12
Details	binding site for residue DST A 302

Chain	Residue
A	PRO8
A	ASP9
A	GLY10
A	MET11
A	ARG12
A	ARG13
A	ALA52
A	PHE72
A	DST301
A	MG303
A	HOH423
A	HOH460

site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 303

Chain	Residue
A	ASP9
A	DST301
A	DST302
A	HOH423
A	HOH460

site_id	AC4
Number of Residues	11
Details	binding site for residue DST B 301

Chain	Residue
B	PRO8
B	ASP9
B	THR51
B	ASN57
B	ARG163
B	ARG169
B	SER171
B	PHE173
B	DST302
B	MG303
F	TYR180

site_id	AC5
Number of Residues	10
Details	binding site for residue DST B 302

Chain	Residue
B	PRO8
B	ASP9
B	GLY10
B	MET11
B	ARG12
B	ARG13
B	TYR26
B	ALA52
B	DST301
B	MG303

site_id	AC6
Number of Residues	3
Details	binding site for residue MG B 303

Chain	Residue
B	ASP9
B	DST301
B	DST302

site_id	AC7
Number of Residues	18
Details	binding site for residue DST C 301

Chain	Residue
C	LEU7
C	PRO8
C	ASP9
C	THR51
C	ALA52
C	ASN57
C	ARG163
C	ARG169
C	SER171
C	PHE173
C	DST302
C	MG303
C	HOH404
C	HOH426
H	TYR180
H	ARG211
H	PHE212
H	GLY213

site_id	AC8
Number of Residues	14
Details	binding site for residue DST C 302

Chain	Residue
C	PRO8
C	ASP9
C	GLY10
C	MET11
C	ARG12
C	ARG13
C	TYR26
C	ALA52
C	ARG60
C	PHE72
C	DST301
C	MG303
C	HOH404
C	HOH426

site_id	AC9
Number of Residues	5
Details	binding site for residue MG C 303

Chain	Residue
C	ASP9
C	DST301
C	DST302
C	HOH404
C	HOH426

site_id	AD1
Number of Residues	13
Details	binding site for residue DST D 301

Chain	Residue
D	DST302
D	MG303
D	HOH411
G	TYR180
D	PRO8
D	ASP9
D	THR51
D	ALA52
D	SER53
D	ARG163
D	ARG169
D	SER171
D	PHE173

site_id	AD2
Number of Residues	14
Details	binding site for residue DST D 302

Chain	Residue
D	PRO8
D	ASP9
D	GLY10
D	MET11
D	ARG12
D	ARG13
D	TYR26
D	ALA52
D	ASN57
D	PHE68
D	DST301
D	MG303
D	HOH411
D	HOH421

site_id	AD3
Number of Residues	5
Details	binding site for residue MG D 303

Chain	Residue
D	ASP9
D	DST301
D	DST302
D	HOH411
D	HOH421

site_id	AD4
Number of Residues	14
Details	binding site for residue DST E 301

Chain	Residue
E	LEU7
E	PRO8
E	ASP9
E	THR51
E	ASN57
E	ARG163
E	ARG169
E	SER171
E	PHE173
E	DST302
E	MG303
E	HOH407
E	HOH424
E	HOH455

site_id	AD5
Number of Residues	12
Details	binding site for residue DST E 302

Chain	Residue
E	PRO8
E	ASP9
E	GLY10
E	MET11
E	ARG12
E	ARG13
E	TYR26
E	ALA52
E	ARG60
E	DST301
E	MG303
E	HOH455

site_id	AD6
Number of Residues	4
Details	binding site for residue MG E 303

Chain	Residue
E	ASP9
E	DST301
E	DST302
E	HOH455

site_id	AD7
Number of Residues	13
Details	binding site for residue DST F 301

Chain	Residue
F	LEU7
F	PRO8
F	ASP9
F	THR51
F	ASN57
F	ARG163
F	ARG169
F	SER171
F	PHE173
F	DST302
F	MG303
F	HOH401
F	HOH402

site_id	AD8
Number of Residues	13
Details	binding site for residue DST F 302

Chain	Residue
F	PRO8
F	ASP9
F	GLY10
F	MET11
F	ARG12
F	ARG13
F	TYR26
F	ALA52
F	ASN57
F	ARG60
F	PHE68
F	DST301
F	MG303

site_id	AD9
Number of Residues	5
Details	binding site for residue MG F 303

Chain	Residue
F	ASP9
F	DST301
F	DST302
F	HOH402
F	HOH431

site_id	AE1
Number of Residues	13
Details	binding site for residue DST G 301

Chain	Residue
G	LEU7
G	PRO8
G	ASP9
G	THR51
G	ARG163
G	ARG169
G	SER171
G	PHE173
G	DST302
G	MG303
G	HOH401
G	HOH403
G	HOH409

site_id	AE2
Number of Residues	11
Details	binding site for residue DST G 302

Chain	Residue
G	PRO8
G	ASP9
G	GLY10
G	MET11
G	ARG12
G	ARG13
G	TYR26
G	ARG60
G	DST301
G	MG303
G	HOH409

site_id	AE3
Number of Residues	4
Details	binding site for residue MG G 303

Chain	Residue
G	ASP9
G	DST301
G	DST302
G	HOH409

site_id	AE4
Number of Residues	15
Details	binding site for residue DST H 301

Chain	Residue
C	TYR180
H	LEU7
H	PRO8
H	ASP9
H	THR51
H	ASN57
H	ARG163
H	ARG169
H	SER171
H	PHE173
H	DST302
H	MG303
H	HOH407
H	HOH452
H	HOH477

site_id	AE5
Number of Residues	12
Details	binding site for residue DST H 302

Chain	Residue
H	PRO8
H	ASP9
H	GLY10
H	MET11
H	ARG12
H	ARG13
H	TYR26
H	ALA52
H	ASN57
H	ARG60
H	DST301
H	MG303

site_id	AE6
Number of Residues	3
Details	binding site for residue MG H 303

Chain	Residue
H	ASP9
H	DST301
H	DST302

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