Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2O1S

1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0005829	cellular_component	cytosol
A	0006744	biological_process	ubiquinone biosynthetic process
A	0008299	biological_process	isoprenoid biosynthetic process
A	0008615	biological_process	pyridoxine biosynthetic process
A	0008661	molecular_function	1-deoxy-D-xylulose-5-phosphate synthase activity
A	0009228	biological_process	thiamine biosynthetic process
A	0016114	biological_process	terpenoid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016744	molecular_function	transketolase or transaldolase activity
A	0019288	biological_process	isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0052865	biological_process	1-deoxy-D-xylulose 5-phosphate biosynthetic process
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0005829	cellular_component	cytosol
B	0006744	biological_process	ubiquinone biosynthetic process
B	0008299	biological_process	isoprenoid biosynthetic process
B	0008615	biological_process	pyridoxine biosynthetic process
B	0008661	molecular_function	1-deoxy-D-xylulose-5-phosphate synthase activity
B	0009228	biological_process	thiamine biosynthetic process
B	0016114	biological_process	terpenoid biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016744	molecular_function	transketolase or transaldolase activity
B	0019288	biological_process	isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
B	0030976	molecular_function	thiamine pyrophosphate binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0052865	biological_process	1-deoxy-D-xylulose 5-phosphate biosynthetic process
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0005829	cellular_component	cytosol
C	0006744	biological_process	ubiquinone biosynthetic process
C	0008299	biological_process	isoprenoid biosynthetic process
C	0008615	biological_process	pyridoxine biosynthetic process
C	0008661	molecular_function	1-deoxy-D-xylulose-5-phosphate synthase activity
C	0009228	biological_process	thiamine biosynthetic process
C	0016114	biological_process	terpenoid biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016744	molecular_function	transketolase or transaldolase activity
C	0019288	biological_process	isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
C	0030976	molecular_function	thiamine pyrophosphate binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0052865	biological_process	1-deoxy-D-xylulose 5-phosphate biosynthetic process
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0005829	cellular_component	cytosol
D	0006744	biological_process	ubiquinone biosynthetic process
D	0008299	biological_process	isoprenoid biosynthetic process
D	0008615	biological_process	pyridoxine biosynthetic process
D	0008661	molecular_function	1-deoxy-D-xylulose-5-phosphate synthase activity
D	0009228	biological_process	thiamine biosynthetic process
D	0016114	biological_process	terpenoid biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016744	molecular_function	transketolase or transaldolase activity
D	0019288	biological_process	isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
D	0030976	molecular_function	thiamine pyrophosphate binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
D	0052865	biological_process	1-deoxy-D-xylulose 5-phosphate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1001

Chain	Residue
A	ASP152
A	ASN181
A	TPP3001
A	HOH3137
A	HOH3138

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 2001

Chain	Residue
A	PRO413
A	GLY464
A	TYR465
A	TYR467

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 1002

Chain	Residue
B	ASP152
B	ASN179
B	ASN181
B	DPO4001
B	HOH4130

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K B 2002

Chain	Residue
B	PRO413
B	GLY464
B	TYR465
B	TYR467

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 1003

Chain	Residue
C	ASP152
C	ASN181
C	LYS284
C	TPP3002
C	HOH3121

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K C 2003

Chain	Residue
C	PRO413
C	GLY464
C	TYR465
C	TYR467

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 1004

Chain	Residue
D	ASP152
D	ASN181
D	DPO4002
D	HOH4113

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D 2004

Chain	Residue
D	PRO413
D	GLY464
D	TYR465
D	TYR467

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE TPP A 3001

Chain	Residue
A	SER52
A	HIS80
A	GLY121
A	HIS122
A	SER123
A	GLY151
A	ASP152
A	GLY153
A	ALA154
A	ASN181
A	TYR288
A	ALA345
A	MSE346
A	ILE368
A	GLU370
A	PHE395
A	ARG398
A	MG1001
A	HOH3100
A	HOH3141
A	HOH3158

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DPO B 4001

Chain	Residue
B	HIS80
B	GLY151
B	ASP152
B	GLY153
B	ALA154
B	ASN181
B	MG1002

site_id	BC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE TPP C 3002

Chain	Residue
C	HIS80
C	GLY121
C	HIS122
C	SER123
C	GLY151
C	ASP152
C	GLY153
C	ALA154
C	ASN181
C	LYS284
C	TYR288
C	ALA345
C	MSE346
C	ILE368
C	GLU370
C	PHE395
C	ARG398
C	MG1003
C	HOH3121
C	HOH3129

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DPO D 4002

Chain	Residue
D	HIS80
D	GLY151
D	ASP152
D	GLY153
D	ALA154
D	ASN181
D	MG1004

Functional Information from PROSITE/UniProt

site_id	PS00801
Number of Residues	20
Details	TRANSKETOLASE_1 Transketolase signature 1. RrylLDsvsrs.SGHFAsgLG

Chain	Residue	Details
A	ARG36-GLY55

site_id	PS00802
Number of Residues	17
Details	TRANSKETOLASE_2 Transketolase signature 2. GADGQTHqGAFdlSylR

Chain	Residue	Details
A	GLY425-ARG441

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:17135236

Chain	Residue	Details
A	GLN81
B	GLN371
C	GLN81
C	GLY153
C	GLU182
C	GLU289
C	GLN371
D	GLN81
D	GLY153
D	GLU182
D	GLU289
A	GLY153
D	GLN371
A	GLU182
A	GLU289
A	GLN371
B	GLN81
B	GLY153
B	GLU182
B	GLU289

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	HIS122
A	ALA154
B	HIS122
B	ALA154
C	HIS122
C	ALA154
D	HIS122
D	ALA154

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
A	GLU370

site_id	CSA10
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
B	PRO253

site_id	CSA11
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
C	PRO253

site_id	CSA12
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
D	PRO253

site_id	CSA13
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
A	PHE248

site_id	CSA14
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
B	PHE248

site_id	CSA15
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
C	PHE248

site_id	CSA16
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
D	PHE248

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
D	GLU370

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
C	GLU370

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
B	GLU370

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
A	HIS431
A	GLU370

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
B	HIS431
B	GLU370

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
C	HIS431
C	GLU370

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
D	HIS431
D	GLU370

site_id	CSA9
Number of Residues	1
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
A	PRO253

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