Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ND7

Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine

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	11
Details	BINDING SITE FOR RESIDUE PNY A 501

Chain	Residue
A	GLY9
A	HOH200
C	GLU135
A	SER10
A	GLN73
A	LEU74
A	THR75
A	TYR99
A	MET106
A	ASN107
A	HOH193

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PNY B 502

Chain	Residue
B	PHE37
B	GLN73
B	LEU74
B	THR75
B	TYR99
B	ILE103
B	MET106
B	ASN107
B	HOH172
B	HOH173
F	GLU135
F	PHE139

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PNY C 503

Chain	Residue
C	GLN73
C	LEU74
C	THR75
C	ARG89
C	TYR99
C	ILE103
C	MET106
C	ASN107
C	HOH182
E	GLU135

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PNY D 504

Chain	Residue
B	LEU132
B	GLU135
D	PRO8
D	GLN73
D	LEU74
D	THR75
D	TYR99
D	ILE103
D	MET106
D	ASN107
D	HOH178
D	HOH192
D	HOH199

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PNY E 505

Chain	Residue
A	GLU135
E	GLY9
E	GLN73
E	LEU74
E	THR75
E	ARG89
E	TYR99
E	MET106
E	ASN107
E	HOH179
E	HOH225

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PNY F 506

Chain	Residue
D	GLU135
F	LEU74
F	THR75
F	TYR99
F	MET106
F	ASN107
F	HOH172
F	HOH182

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00151

Chain	Residue	Details
E	SER10
E	LYS42
E	ARG89
F	SER10
F	LYS42
F	ARG89
A	SER10
A	LYS42
A	ARG89
B	SER10
B	LYS42
B	ARG89
C	SER10
C	LYS42
C	ARG89
D	SER10
D	LYS42
D	ARG89

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00151, ECO:0000269\|PubMed:21912874, ECO:0007744\|PDB:3ND6

Chain	Residue	Details
E	GLU100
E	TYR125
F	HIS18
F	GLY90
F	GLU100
F	TYR125
A	HIS18
A	GLY90
A	GLU100
A	TYR125
B	HIS18
B	GLY90
B	GLU100
B	TYR125
C	HIS18
C	GLY90
C	GLU100
C	TYR125
D	HIS18
D	GLY90
D	GLU100
D	TYR125
E	HIS18
E	GLY90

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00151, ECO:0000305\|PubMed:21912874, ECO:0007744\|PDB:3ND7

Chain	Residue	Details
A	THR75
B	THR75
C	THR75
D	THR75
E	THR75
F	THR75

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Transition state stabilizer => ECO:0000255\|HAMAP-Rule:MF_00151

Chain	Residue	Details
F	HIS18
A	HIS18
B	HIS18
C	HIS18
D	HIS18
E	HIS18

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