Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8XKF

Crystal structure of Helicobacter pylori IspDF with substrate CTP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008299	biological_process	isoprenoid biosynthetic process
A	0008685	molecular_function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
A	0016114	biological_process	terpenoid biosynthetic process
A	0016779	molecular_function	nucleotidyltransferase activity
A	0016829	molecular_function	lyase activity
A	0019288	biological_process	isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
A	0046872	molecular_function	metal ion binding
A	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
B	0008299	biological_process	isoprenoid biosynthetic process
B	0008685	molecular_function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
B	0016114	biological_process	terpenoid biosynthetic process
B	0016779	molecular_function	nucleotidyltransferase activity
B	0016829	molecular_function	lyase activity
B	0019288	biological_process	isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
B	0046872	molecular_function	metal ion binding
B	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
C	0008299	biological_process	isoprenoid biosynthetic process
C	0008685	molecular_function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
C	0016114	biological_process	terpenoid biosynthetic process
C	0016779	molecular_function	nucleotidyltransferase activity
C	0016829	molecular_function	lyase activity
C	0019288	biological_process	isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
C	0046872	molecular_function	metal ion binding
C	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
D	0008299	biological_process	isoprenoid biosynthetic process
D	0008685	molecular_function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
D	0016114	biological_process	terpenoid biosynthetic process
D	0016779	molecular_function	nucleotidyltransferase activity
D	0016829	molecular_function	lyase activity
D	0019288	biological_process	isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
D	0046872	molecular_function	metal ion binding
D	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
E	0008299	biological_process	isoprenoid biosynthetic process
E	0008685	molecular_function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
E	0016114	biological_process	terpenoid biosynthetic process
E	0016779	molecular_function	nucleotidyltransferase activity
E	0016829	molecular_function	lyase activity
E	0019288	biological_process	isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
E	0046872	molecular_function	metal ion binding
E	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
F	0008299	biological_process	isoprenoid biosynthetic process
F	0008685	molecular_function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
F	0016114	biological_process	terpenoid biosynthetic process
F	0016779	molecular_function	nucleotidyltransferase activity
F	0016829	molecular_function	lyase activity
F	0019288	biological_process	isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
F	0046872	molecular_function	metal ion binding
F	0050518	molecular_function	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity

Functional Information from PROSITE/UniProt

site_id	PS01295
Number of Residues	8
Details	ISPD 4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature. TLTSDVAR

Chain	Residue	Details
A	THR126-ARG133

site_id	PS01350
Number of Residues	16
Details	ISPF 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase signature. SDGDALlHAviDAilG

Chain	Residue	Details
A	SER281-GLY296

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	54
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01520

Chain	Residue	Details
A	ASP254
B	ASP254
B	HIS256
B	HIS280
B	HIS288
B	ASP302
B	PHE307
B	THR378
B	PHE385
B	LYS388
C	ASP254
A	HIS256
C	HIS256
C	HIS280
C	HIS288
C	ASP302
C	PHE307
C	THR378
C	PHE385
C	LYS388
D	ASP254
D	HIS256
A	HIS280
D	HIS280
D	HIS288
D	ASP302
D	PHE307
D	THR378
D	PHE385
D	LYS388
E	ASP254
E	HIS256
E	HIS280
A	HIS288
E	HIS288
E	ASP302
E	PHE307
E	THR378
E	PHE385
E	LYS388
F	ASP254
F	HIS256
F	HIS280
F	HIS288
A	ASP302
F	ASP302
F	PHE307
F	THR378
F	PHE385
F	LYS388
A	PHE307
A	THR378
A	PHE385
A	LYS388

site_id	SWS_FT_FI2
Number of Residues	24
Details	SITE: Transition state stabilizer => ECO:0000255\|HAMAP-Rule:MF_01520

Chain	Residue	Details
A	ARG48
C	LYS55
C	HIS280
C	THR379
D	ARG48
D	LYS55
D	HIS280
D	THR379
E	ARG48
E	LYS55
E	HIS280
A	LYS55
E	THR379
F	ARG48
F	LYS55
F	HIS280
F	THR379
A	HIS280
A	THR379
B	ARG48
B	LYS55
B	HIS280
B	THR379
C	ARG48

site_id	SWS_FT_FI3
Number of Residues	12
Details	SITE: Positions MEP for the nucleophilic attack => ECO:0000255\|HAMAP-Rule:MF_01520

Chain	Residue	Details
A	ARG175
E	LYS227
F	ARG175
F	LYS227
A	LYS227
B	ARG175
B	LYS227
C	ARG175
C	LYS227
D	ARG175
D	LYS227
E	ARG175

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