1GN8

PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE IN COMPLEX WITH Mn2+ATP FROM ESCHERICHIA COLI

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	0005515	molecular_function	protein binding
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	0042802	molecular_function	identical protein binding
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
B	0005515	molecular_function	protein binding
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	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 603

Chain	Residue
A	SER121
A	LYS122
A	HOH2113
A	HOH2114
B	HIS104
B	ARG107

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MN A 802

Chain	Residue
A	ATP700

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 601

Chain	Residue
B	SER41
B	ARG137
B	HIS138
B	HOH2031
B	SER39
B	PRO40

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 602

Chain	Residue
A	HIS104
A	ARG107
B	SER121
B	LYS122
B	HOH2128
B	HOH2129

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site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MN B 801

Chain	Residue
B	ATP600

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site_id	AC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ATP A 700

Chain	Residue
A	TYR7
A	THR10
A	PHE11
A	GLY17
A	HIS18
A	ILE21
A	ARG88
A	GLY89
A	ARG91
A	PRO120
A	TRP124
A	ILE127
A	SER128
A	SER129
A	SER130
A	MN802
A	HOH2011
A	HOH2063
A	HOH2089
A	HOH2115
A	HOH2116
A	HOH2117
A	HOH2118

---

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP B 600

Chain	Residue
B	TYR7
B	THR10
B	PHE11
B	GLY17
B	HIS18
B	ILE21
B	ARG88
B	GLY89
B	ARG91
B	GLU99
B	PRO120
B	TRP124
B	ILE127
B	SER128
B	SER129
B	SER130
B	MN801
B	HOH2013
B	HOH2104
B	HOH2126
B	HOH2127

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:11812124, ECO:0000269|PubMed:12837781, ECO:0007744|PDB:1H1T, ECO:0007744|PDB:1QJC

Chain	Residue	Details
A	THR10
A	LYS42
A	MET74
B	THR10
B	LYS42
B	MET74

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1GN8

Chain	Residue	Details
A	HIS18
B	TYR7
A	GLY89
A	GLU99
A	TRP124
B	HIS18
B	GLY89
B	GLU99
B	TRP124
A	TYR7

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1QJC

Chain	Residue	Details
A	ARG88
B	ARG88

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000305|PubMed:11812124

Chain	Residue	Details
A	HIS18
B	HIS18

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 299

Chain	Residue	Details
A	HIS18	electrostatic stabiliser, hydrogen bond donor
A	LYS42	attractive charge-charge interaction, electrostatic stabiliser
A	ARG91	attractive charge-charge interaction, electrostatic stabiliser
A	SER129	electrostatic stabiliser, hydrogen bond donor

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 299

Chain	Residue	Details
B	HIS18	electrostatic stabiliser, hydrogen bond donor
B	LYS42	attractive charge-charge interaction, electrostatic stabiliser
B	ARG91	attractive charge-charge interaction, electrostatic stabiliser
B	SER129	electrostatic stabiliser, hydrogen bond donor

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