Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ND6

Crystal structure of phosphopantetheine adenylyltransferase (PPAT) in complex with ATP from Enterococcus faecalis

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	21
Details	BINDING SITE FOR RESIDUE ATP A 961

Chain	Residue
A	PHE7
A	TYR125
A	VAL128
A	SER129
A	SER130
A	SER131
A	HOH185
A	HOH192
A	HOH200
A	HOH218
A	HOH260
A	GLY17
A	HOH304
A	HOH319
A	HIS18
A	LEU21
A	ARG89
A	GLY90
A	ARG92
A	GLU100
A	ALA121

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ATP B 962

Chain	Residue
B	PHE7
B	GLY9
B	SER10
B	PHE11
B	GLY17
B	HIS18
B	LEU21
B	ARG89
B	GLY90
B	ASP96
B	GLU100
B	ALA121
B	TYR125
B	VAL128
B	SER129
B	SER130
B	SER131
B	HOH187
B	HOH190
B	HOH194
B	HOH202
B	HOH209
B	HOH212
B	HOH264
B	HOH344

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ATP C 963

Chain	Residue
C	PHE7
C	GLY9
C	SER10
C	GLY17
C	HIS18
C	LEU21
C	ARG89
C	GLY90
C	GLU100
C	ALA121
C	TYR125
C	VAL128
C	SER129
C	SER130
C	SER131
C	HOH183
C	HOH185
C	HOH189
C	HOH190
C	HOH215
C	HOH332
C	HOH366
C	HOH413

site_id	AC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ATP D 964

Chain	Residue
D	PHE7
D	GLY9
D	SER10
D	PHE11
D	GLY17
D	HIS18
D	LEU21
D	ARG89
D	GLY90
D	ARG92
D	ASP96
D	GLU100
D	ALA121
D	TYR125
D	VAL128
D	SER129
D	SER130
D	SER131
D	HOH178
D	HOH193
D	HOH196
D	HOH292
D	HOH309
D	HOH320
D	HOH323

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP E 965

Chain	Residue
E	LEU21
E	ARG89
E	GLY90
E	GLU100
E	ALA121
E	TYR125
E	VAL128
E	SER129
E	SER130
E	SER131
E	HOH174
E	HOH182
E	HOH206
E	HOH233
E	PHE7
E	GLY9
E	SER10
E	GLY17
E	HIS18

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP F 966

Chain	Residue
F	PHE7
F	SER10
F	PHE11
F	GLY17
F	HIS18
F	ARG89
F	GLY90
F	GLU100
F	ALA121
F	TYR125
F	VAL128
F	SER129
F	SER130
F	SER131
F	HOH175
F	HOH190
F	HOH200
F	HOH365
F	HOH392

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21912874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ND6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21912874","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3ND7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
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)