5CQB

Crystal structure of E. coli undecaprenyl pyrophosphate synthase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008360	biological_process	regulation of cell shape
A	0008834	molecular_function	di-trans,poly-cis-undecaprenyl-diphosphate synthase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
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	0036094	molecular_function	small molecule binding
A	0042803	molecular_function	protein homodimerization activity
A	0043164	biological_process	Gram-negative-bacterium-type cell wall biogenesis
A	0045547	molecular_function	dehydrodolichyl diphosphate synthase activity
A	0046872	molecular_function	metal ion binding
A	0051301	biological_process	cell division
A	0071555	biological_process	cell wall organization
B	0000287	molecular_function	magnesium ion binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008360	biological_process	regulation of cell shape
B	0008834	molecular_function	di-trans,poly-cis-undecaprenyl-diphosphate synthase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
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	0036094	molecular_function	small molecule binding
B	0042803	molecular_function	protein homodimerization activity
B	0043164	biological_process	Gram-negative-bacterium-type cell wall biogenesis
B	0045547	molecular_function	dehydrodolichyl diphosphate synthase activity
B	0046872	molecular_function	metal ion binding
B	0051301	biological_process	cell division
B	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue PGE A 301

Chain	Residue
A	PHE41
A	ALA45
A	LYS48
A	GLN163
B	VAL162
B	GLN163

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Functional Information from PROSITE/UniProt

site_id	PS01066
Number of Residues	18
Details	UPP_SYNTHASE Undecaprenyl pyrophosphate synthase family signature. DLVIRTGGehRiSnFLLW

Chain	Residue	Details
A	ASP190-TRP207

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE:

Chain	Residue	Details
A	ASP26
B	ASP26

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250

Chain	Residue	Details
A	ASN74
B	ASN74

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	ASP26
A	HIS199
A	ARG200
A	GLU213
B	ASP26
B	HIS199
B	ARG200
B	GLU213

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site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:15044730

Chain	Residue	Details
A	TRP31
A	TRP75
B	TRP31
B	TRP75

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:15044730

Chain	Residue	Details
A	ARG39
A	HIS43
A	ARG77
A	ARG194
B	ARG39
B	HIS43
B	ARG77
B	ARG194

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site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	SER71
B	SER71

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site_id	SWS_FT_FI7
Number of Residues	2
Details	SITE: Required for continued chain elongation

Chain	Residue	Details
A	ALA69
B	ALA69

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site_id	SWS_FT_FI8
Number of Residues	2
Details	SITE: Important for determining product length

Chain	Residue	Details
A	LEU137
B	LEU137

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