3NBA

Phosphopantetheine Adenylyltranferase from Mycobacterium tuberculosis in complex with adenosine-5'-[(alpha,beta)-methyleno]triphosphate (AMPCPP)

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
A	0034214	biological_process	protein hexamerization
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
B	0034214	biological_process	protein hexamerization
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
C	0034214	biological_process	protein hexamerization
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
D	0034214	biological_process	protein hexamerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE APC A 200

Chain	Residue
A	SER9
A	VAL125
A	SER126
A	SER127
A	SER128
A	MG158
A	HOH176
A	HOH177
A	HOH245
A	HOH251
A	HOH256
A	PHE10
A	HOH257
A	GLY16
A	HIS17
A	ILE20
A	GLY88
A	ARG90
A	THR118
A	TYR122

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE APC B 200

Chain	Residue
B	GLY8
B	SER9
B	PHE10
B	GLY16
B	HIS17
B	ILE20
B	LYS87
B	GLY88
B	ARG90
B	THR118
B	TYR122
B	VAL125
B	SER127
B	SER128
B	HOH163
B	HOH164
B	HOH254
B	HOH281

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 158

Chain	Residue
A	HOH177
A	APC200

---

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE APC C 200

Chain	Residue
C	SER9
C	PHE10
C	GLY16
C	HIS17
C	ILE20
C	GLY88
C	ARG90
C	THR118
C	TYR122
C	VAL125
C	SER126
C	SER127
C	SER128
C	MG158
C	HOH166
C	HOH170
C	HOH248

---

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE APC D 200

Chain	Residue
D	PRO7
D	GLY8
D	SER9
D	PHE10
D	GLY16
D	HIS17
D	ILE20
D	GLY88
D	ARG90
D	THR118
D	TYR122
D	VAL125
D	SER126
D	SER127
D	SER128
D	MG158
D	HOH163
D	HOH175
D	HOH252
D	HOH261
D	HOH265

---

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG C 158

Chain	Residue
C	APC200

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG D 158

Chain	Residue
D	APC200

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23151631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20851704","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3NBA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UC5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20851704","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NBK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23151631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UC5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20851704","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NBK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23151631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20851704","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3NBA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UC5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"PubMed","id":"21969609","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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