Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4NAH

Inhibitors of 4-Phosphopanthetheine Adenylyltransferase (PPAT)

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	19
Details	BINDING SITE FOR RESIDUE AGS A 201

Chain	Residue
A	SER11
A	GLU100
A	SER121
A	TYR125
A	ILE128
A	SER129
A	SER130
A	SER131
A	2VJ203
A	HOH302
A	HOH313
A	PHE12
A	GLY18
A	HIS19
A	ILE22
A	ARG89
A	GLY90
A	ARG92
A	ASP96

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 2VJ A 202

Chain	Residue
A	GLU135
A	VAL136
A	TYR139
A	HOH301
C	CYS36
C	LYS43
C	GLY73
C	LEU74
C	LEU75
C	ARG89
C	TYR99
C	ASN107
C	HOH301

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 2VJ A 203

Chain	Residue
A	PRO9
A	SER11
A	CYS36
A	VAL37
A	LEU38
A	GLY73
A	LEU75
A	ARG89
A	TYR99
A	MET106
A	ASN107
A	AGS201
A	HOH304
A	HOH306
B	GLU135
B	TYR139
B	HOH307

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AGS B 201

Chain	Residue
B	SER11
B	PHE12
B	GLY18
B	HIS19
B	ARG89
B	GLY90
B	ARG92
B	GLU100
B	SER121
B	TYR125
B	ILE128
B	SER129
B	SER130
B	SER131
B	HOH312

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 2VJ B 202

Chain	Residue
B	PRO9
B	CYS36
B	VAL37
B	LEU38
B	GLY73
B	LEU74
B	LEU75
B	ARG89
B	TYR99
B	MET106
B	ASN107
B	HOH301
C	GLU135

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE AGS C 201

Chain	Residue
C	PRO9
C	SER11
C	PHE12
C	GLY18
C	HIS19
C	ILE22
C	ARG89
C	GLY90
C	ARG92
C	GLU100
C	SER121
C	TYR125
C	ILE128
C	SER129
C	SER130
C	SER131
C	HOH302

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE AGS D 201

Chain	Residue
D	ILE22
D	ARG89
D	GLY90
D	ARG92
D	GLU100
D	SER121
D	TYR125
D	ILE128
D	SER129
D	SER130
D	SER131
D	HOH303
D	HOH305
D	PRO9
D	SER11
D	PHE12
D	GLY18
D	HIS19

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 2VJ D 202

Chain	Residue
D	PRO9
D	GLY10
D	CYS36
D	VAL37
D	GLY73
D	LEU75
D	ARG89
D	TYR99
D	MET106
D	ASN107
D	HOH301
E	GLU135

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE AGS E 201

Chain	Residue
E	SER11
E	PHE12
E	GLY18
E	HIS19
E	ARG89
E	GLY90
E	ARG92
E	ASP96
E	GLU100
E	SER121
E	TYR125
E	ILE128
E	SER129
E	SER130
E	SER131
E	HOH303

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AGS F 201

Chain	Residue
F	GLY10
F	SER11
F	PHE12
F	GLY18
F	HIS19
F	ILE22
F	ARG89
F	GLY90
F	ARG92
F	SER121
F	TYR125
F	ILE128
F	SER129
F	SER130
F	SER131

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 2VJ F 202

Chain	Residue
E	PRO9
E	CYS36
E	GLY73
E	LEU75
E	TYR99
E	LEU103
E	ASN107
F	GLU135
F	VAL136
F	TYR139

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 2VJ F 203

Chain	Residue
D	GLU135
D	TYR139
F	PRO9
F	CYS36
F	GLY73
F	LEU74
F	LEU75
F	ARG89
F	TYR99
F	GLU100
F	ASN107
F	HOH302

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24041904","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NAT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NAU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24041904","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NAU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24041904","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NAH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24041904","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NAH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NAU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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