Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3OTW

Structural and Functional Studies of Helicobacter pylori Wild-Type and Mutated Proteins Phosphopantetheine adenylyltransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0009058	biological_process	biosynthetic process
A	0015937	biological_process	coenzyme A biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0009058	biological_process	biosynthetic process
B	0015937	biological_process	coenzyme A biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0009058	biological_process	biosynthetic process
C	0015937	biological_process	coenzyme A biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016779	molecular_function	nucleotidyltransferase activity
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0009058	biological_process	biosynthetic process
D	0015937	biological_process	coenzyme A biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016779	molecular_function	nucleotidyltransferase activity
E	0000166	molecular_function	nucleotide binding
E	0003824	molecular_function	catalytic activity
E	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0009058	biological_process	biosynthetic process
E	0015937	biological_process	coenzyme A biosynthetic process
E	0016740	molecular_function	transferase activity
E	0016779	molecular_function	nucleotidyltransferase activity
F	0000166	molecular_function	nucleotide binding
F	0003824	molecular_function	catalytic activity
F	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0009058	biological_process	biosynthetic process
F	0015937	biological_process	coenzyme A biosynthetic process
F	0016740	molecular_function	transferase activity
F	0016779	molecular_function	nucleotidyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 158

Chain	Residue
B	HIS38
B	SER47
B	LEU48
B	HOH172
B	HOH179
B	HOH506

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 158

Chain	Residue
D	HOH510
D	HIS38
D	SER47
D	LEU48

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 158

Chain	Residue
A	HIS38
A	LEU48
A	HOH173
A	HOH181
A	HOH283

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 159

Chain	Residue
B	SER130
B	ARG133
B	HOH167

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 E 158

Chain	Residue
E	ARG133

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 158

Chain	Residue
C	HIS38
C	SER47
C	LEU48
C	HOH168
C	HOH186

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 159

Chain	Residue
E	HIS38
E	SER47
E	LEU48
E	HOH274

site_id	AC8
Number of Residues	30
Details	BINDING SITE FOR RESIDUE COA B 160

Chain	Residue
B	GLY9
B	THR10
B	THR15
B	GLY17
B	HIS18
B	ALA37
B	LYS42
B	GLY72
B	LEU73
B	LEU74
B	ARG88
B	ARG91
B	TYR98
B	ASN106
B	ILE127
B	SER128
B	SER129
B	SER130
B	ARG133
B	HOH161
B	HOH162
B	HOH180
B	HOH194
B	HOH195
B	HOH250
B	HOH472
B	HOH519
B	HOH601
C	SER134
C	HIS138

site_id	AC9
Number of Residues	29
Details	BINDING SITE FOR RESIDUE COA A 159

Chain	Residue
A	GLY9
A	THR10
A	THR15
A	GLY17
A	HIS18
A	ALA37
A	LYS42
A	GLY72
A	LEU73
A	LEU74
A	ARG88
A	ARG91
A	TYR98
A	ASN106
A	ILE127
A	SER128
A	SER129
A	SER130
A	ARG133
A	HOH162
A	HOH167
A	HOH174
A	HOH219
A	HOH411
A	HOH416
A	HOH417
A	HOH523
D	SER134
D	HIS138

site_id	BC1
Number of Residues	30
Details	BINDING SITE FOR RESIDUE COA C 159

Chain	Residue
C	TYR98
C	ASN106
C	ILE127
C	SER128
C	SER129
C	SER130
C	ARG133
C	HOH160
C	HOH173
C	HOH180
C	HOH182
C	HOH183
C	HOH453
C	HOH454
C	HOH462
C	HOH463
E	SER134
E	HIS138
C	GLY9
C	THR10
C	THR15
C	GLY17
C	HIS18
C	ALA37
C	LYS42
C	GLY72
C	LEU73
C	LEU74
C	ARG88
C	ARG91

site_id	BC2
Number of Residues	30
Details	BINDING SITE FOR RESIDUE COA D 159

Chain	Residue
D	GLY9
D	THR10
D	THR15
D	GLY17
D	HIS18
D	ALA37
D	LYS42
D	GLY72
D	LEU73
D	LEU74
D	ARG88
D	ARG91
D	TYR98
D	ASN106
D	ILE127
D	SER128
D	SER129
D	SER130
D	ARG133
D	HOH164
D	HOH178
D	HOH423
D	HOH443
D	HOH465
D	HOH466
D	HOH509
D	HOH578
F	SER134
F	HIS138
F	HOH449

site_id	BC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE COA E 160

Chain	Residue
E	GLY9
E	THR10
E	THR15
E	GLY17
E	HIS18
E	ALA37
E	LYS42
E	GLY72
E	LEU73
E	LEU74
E	ARG88
E	ARG91
E	TYR98
E	ASN106
E	ILE127
E	SER128
E	SER129
E	SER130
E	ARG133
E	HOH162
E	HOH252
E	HOH294
E	HOH303
E	HOH306
E	HOH420
E	HOH451
E	HOH580

site_id	BC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE COA F 158

Chain	Residue
F	GLY9
F	THR10
F	THR15
F	GLY17
F	HIS18
F	ALA37
F	LYS42
F	PHE70
F	GLY72
F	LEU73
F	LEU74
F	ARG88
F	ARG91
F	TYR98
F	ASN106
F	ILE127
F	SER128
F	SER129
F	ARG133
F	HOH160
F	HOH164
F	HOH168
F	HOH290
F	HOH367
F	HOH413
F	HOH467

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21527250","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3OTW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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