Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5TS2

Crystal structure of a phosphopantetheine adenylyltransferase (CoaD, PPAT) from Pseudomonas aeruginosa bound to dephospho coenzyme A

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	0008771	molecular_function	[citrate (pro-3S)-lyase] ligase activity
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	0008771	molecular_function	[citrate (pro-3S)-lyase] ligase activity
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	0008771	molecular_function	[citrate (pro-3S)-lyase] ligase activity
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	0008771	molecular_function	[citrate (pro-3S)-lyase] ligase activity
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	0008771	molecular_function	[citrate (pro-3S)-lyase] ligase activity
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	0008771	molecular_function	[citrate (pro-3S)-lyase] ligase activity
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	20
Details	binding site for residue COD A 201

Chain	Residue
A	TYR6
A	LEU73
A	ARG87
A	GLY88
A	ARG90
A	LEU101
A	ASN105
A	PRO119
A	TYR123
A	ILE126
A	HOH315
A	PRO7
E	LEU137
A	GLY8
A	THR9
A	PHE10
A	GLY16
A	HIS17
A	THR71
A	LEU72

site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 202

Chain	Residue
A	HIS-3
A	HIS-5
C	HIS-3
C	HIS-5
E	HIS-3
E	HIS-5

site_id	AC3
Number of Residues	2
Details	binding site for residue CL A 203

Chain	Residue
A	SER127
A	THR129

site_id	AC4
Number of Residues	22
Details	binding site for residue COD B 201

Chain	Residue
B	TYR6
B	PRO7
B	GLY8
B	THR9
B	PHE10
B	GLY16
B	HIS17
B	PHE69
B	LEU72
B	LEU73
B	ARG87
B	GLY88
B	ARG90
B	TYR97
B	GLU98
B	ASN105
B	PRO119
B	TYR123
B	ILE126
B	HOH301
B	HOH303
B	HOH306

site_id	AC5
Number of Residues	2
Details	binding site for residue CL B 202

Chain	Residue
B	SER127
B	THR129

site_id	AC6
Number of Residues	3
Details	binding site for residue CL B 203

Chain	Residue
B	ALA109
B	PRO110
B	ASP111

site_id	AC7
Number of Residues	19
Details	binding site for residue COD C 201

Chain	Residue
A	LEU137
C	TYR6
C	PRO7
C	GLY8
C	THR9
C	PHE10
C	GLY16
C	HIS17
C	LYS41
C	LEU72
C	LEU73
C	ARG87
C	GLY88
C	ARG90
C	TYR97
C	PRO119
C	TYR123
C	ILE126
C	HOH325

site_id	AC8
Number of Residues	2
Details	binding site for residue CL C 202

Chain	Residue
C	SER127
C	THR129

site_id	AC9
Number of Residues	3
Details	binding site for residue CL C 203

Chain	Residue
C	ALA109
C	PRO110
C	ASP111

site_id	AD1
Number of Residues	3
Details	binding site for residue CL C 204

Chain	Residue
C	HIS-5
C	HIS-4
C	HIS0

site_id	AD2
Number of Residues	22
Details	binding site for residue COD D 201

Chain	Residue
D	ILE126
D	HOH326
D	HOH330
F	LEU130
F	GLU133
D	TYR6
D	PRO7
D	GLY8
D	THR9
D	PHE10
D	GLY16
D	HIS17
D	THR71
D	LEU72
D	LEU73
D	ARG87
D	GLY88
D	ARG90
D	LEU101
D	ASN105
D	PRO119
D	TYR123

site_id	AD3
Number of Residues	2
Details	binding site for residue CL D 202

Chain	Residue
D	SER127
D	THR129

site_id	AD4
Number of Residues	3
Details	binding site for residue CL D 203

Chain	Residue
D	ALA109
D	PRO110
D	ASP111

site_id	AD5
Number of Residues	21
Details	binding site for residue COD E 201

Chain	Residue
C	LEU130
C	LEU137
E	TYR6
E	PRO7
E	GLY8
E	THR9
E	PHE10
E	GLY16
E	HIS17
E	PHE69
E	LEU72
E	LEU73
E	ARG87
E	GLY88
E	ARG90
E	GLU98
E	LEU101
E	PRO119
E	TYR123
E	ILE126
E	HOH323

site_id	AD6
Number of Residues	5
Details	binding site for residue CA E 202

Chain	Residue
C	HOH322
E	VAL64
E	HOH311
E	HOH319
E	HOH330

site_id	AD7
Number of Residues	3
Details	binding site for residue CL E 203

Chain	Residue
E	ALA109
E	PRO110
E	ASP111

site_id	AD8
Number of Residues	25
Details	binding site for residue COD F 201

Chain	Residue
B	GLU133
B	LEU137
F	TYR6
F	PRO7
F	GLY8
F	THR9
F	PHE10
F	GLY16
F	HIS17
F	LYS41
F	LEU72
F	LEU73
F	ARG87
F	GLY88
F	ARG90
F	GLU98
F	LEU101
F	ASN105
F	PRO119
F	TYR123
F	ILE126
F	HOH304
F	HOH310
F	HOH311
F	HOH316

site_id	AD9
Number of Residues	2
Details	binding site for residue CL F 202

Chain	Residue
F	SER127
F	THR129

site_id	AE1
Number of Residues	3
Details	binding site for residue CL F 203

Chain	Residue
F	ALA109
F	PRO110
F	ASP111

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	90
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
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)