1B6T

PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE IN COMPLEX WITH 3'-DEPHOSPHO-COA 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	8
Details	BINDING SITE FOR RESIDUE SO4 B 501

Chain	Residue
B	SER39
B	PRO40
B	SER41
B	ARG137
B	HIS138
B	HOH3048
B	HOH3086
B	HOH3154

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 502

Chain	Residue
A	LYS122
A	HOH561
A	HOH564
A	HOH609
B	HIS104
B	ARG107
A	SER121

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 503

Chain	Residue
A	HIS104
A	ARG107
B	SER121
B	LYS122
B	HOH3029
B	HOH3087
B	HOH3125
B	HOH3153

---

site_id	AC4
Number of Residues	31
Details	BINDING SITE FOR RESIDUE COD B 3000

Chain	Residue
B	TYR7
B	PRO8
B	GLY9
B	THR10
B	PHE11
B	GLY17
B	HIS18
B	ILE21
B	ALA37
B	LYS42
B	LEU73
B	MET74
B	ARG88
B	GLY89
B	ARG91
B	ASP95
B	GLU99
B	LEU102
B	MET105
B	ASN106
B	PRO120
B	TRP124
B	ILE127
B	GLU134
B	HIS138
B	HOH3005
B	HOH3016
B	HOH3032
B	HOH3081
B	HOH3146
B	HOH3154

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:11812124, ECO:0007744|PDB:1GN8

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

---

site_id	SWS_FT_FI2
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_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	CSA1
Number of Residues	3
Details

Chain	Residue	Details
A	HIS18
A	SER129
A	ARG91

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site_id	CSA2
Number of Residues	3
Details

Chain	Residue	Details
B	HIS18
B	SER129
B	ARG91

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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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