3NBK

Phosphopantetheine Adenylyltransferase from Mycobacterium tuberculosis in complex with 4'-phosphopantetheine

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	18
Details	BINDING SITE FOR RESIDUE PNS A 200

Chain	Residue
A	GLY8
A	HOH186
A	HOH203
A	HOH204
A	HOH222
A	HOH355
A	HOH357
A	HOH412
A	HOH720
A	HOH1008
A	SER9
A	GLY71
A	LEU72
A	VAL73
A	ASN105
A	GLU132
A	HOH172
A	HOH177

---

site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PNS B 200

Chain	Residue
B	GLY8
B	SER9
B	GLY71
B	LEU72
B	VAL73
B	ASN105
B	GLU132
B	LEU136
B	HOH175
B	HOH178
B	HOH191
B	HOH194
B	HOH195
B	HOH203
B	HOH279
B	HOH337
B	HOH347
B	HOH379
B	HOH648
B	HOH687

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PNS C 200

Chain	Residue
C	GLY8
C	SER9
C	GLY71
C	LEU72
C	VAL73
C	ASN105
C	GLU132
C	HOH168
C	HOH172
C	HOH182
C	HOH188
C	HOH194
C	HOH205
C	HOH291
C	HOH354
C	HOH452
C	HOH518
C	HOH642

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PNS D 200

Chain	Residue
D	GLY8
D	SER9
D	GLY71
D	LEU72
D	VAL73
D	ASN105
D	GLU132
D	HOH171
D	HOH179
D	HOH210
D	HOH322
D	HOH325
D	HOH416
D	HOH436
D	HOH531
D	HOH807

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NI C 162

Chain	Residue
C	ARG-3
C	HIS0
C	ASP29
D	ARG-3
D	HIS0
D	ASP29
D	HOH255

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NI A 162

Chain	Residue
A	HIS0
A	ASP29
B	HIS0
B	ASP29

---

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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