6CCO

Crystal structure of E.coli Phosphopantetheine Adenylyltransferase (PPAT/CoaD) in complex with 3-((1S,2S)-2-(4-hydroxy-1H-benzo[d]imidazol-2-yl)cyclopentyl)benzoic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0016779	molecular_function	nucleotidyltransferase activity
A	0042802	molecular_function	identical protein 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	0016779	molecular_function	nucleotidyltransferase activity
B	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue EXV A 201

Chain	Residue
A	GLY9
A	GLU134
A	VAL135
A	HIS138
A	HOH356
A	ALA37
A	ASP72
A	LEU73
A	MET74
A	ALA75
A	ARG88
A	LEU102
A	ASN106

---

site_id	AC2
Number of Residues	7
Details	binding site for residue SO4 A 202

Chain	Residue
A	SER121
A	LYS122
A	HOH301
A	HOH303
A	HOH307
B	HIS104
B	ARG107

---

site_id	AC3
Number of Residues	6
Details	binding site for residue SO4 A 203

Chain	Residue
A	HIS18
A	ARG91
A	SER128
A	SER129
A	HOH302
A	HOH330

---

site_id	AC4
Number of Residues	7
Details	binding site for residue SO4 B 201

Chain	Residue
B	HIS18
B	ARG91
B	SER128
B	SER129
B	HOH301
B	HOH303
B	HOH304

---

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 B 202

Chain	Residue
B	GLY9
B	THR10
B	LYS42
B	ARG88
B	HOH301

---

site_id	AC6
Number of Residues	7
Details	binding site for residue SO4 B 203

Chain	Residue
B	SER39
B	PRO40
B	SER41
B	ARG137
B	HIS138
B	HOH328
B	HOH330

---

site_id	AC7
Number of Residues	7
Details	binding site for residue SO4 B 204

Chain	Residue
A	HIS104
A	ARG107
B	SER121
B	LYS122
B	HOH302
B	HOH305
B	HOH307

---

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

---

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

---

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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