1ESM

STRUCTURAL BASIS FOR THE FEEDBACK REGULATION OF ESCHERICHIA COLI PANTOTHENATE KINASE BY COENZYME A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004594	molecular_function	pantothenate kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0015937	biological_process	coenzyme A biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0042803	molecular_function	protein homodimerization activity
A	0050165	molecular_function	pantetheine kinase activity
B	0000166	molecular_function	nucleotide binding
B	0004594	molecular_function	pantothenate kinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0015937	biological_process	coenzyme A biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0042803	molecular_function	protein homodimerization activity
B	0050165	molecular_function	pantetheine kinase activity
C	0000166	molecular_function	nucleotide binding
C	0004594	molecular_function	pantothenate kinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0015937	biological_process	coenzyme A biosynthetic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0042803	molecular_function	protein homodimerization activity
C	0050165	molecular_function	pantetheine kinase activity
D	0000166	molecular_function	nucleotide binding
D	0004594	molecular_function	pantothenate kinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0015937	biological_process	coenzyme A biosynthetic process
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0042803	molecular_function	protein homodimerization activity
D	0050165	molecular_function	pantetheine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE COA A 401

Chain	Residue
A	GLY41
A	HIS177
A	TYR180
A	LEU201
A	TYR240
A	ARG243
A	PHE247
A	PHE252
A	ASN282
C	ARG38
A	ILE42
A	VAL97
A	ALA98
A	LYS101
A	SER102
A	ARG106
A	LYS145
A	TYR175

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site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE COA C 402

Chain	Residue
A	ARG38
C	GLY41
C	ILE42
C	VAL97
C	ALA98
C	LYS101
C	SER102
C	ARG106
C	LYS145
C	HIS177
C	TYR180
C	LEU201
C	TYR240
C	ARG243
C	PHE247
C	PHE252
C	ASN282
C	HOH577

---

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE COA D 403

Chain	Residue
B	ARG38
D	GLY41
D	ILE42
D	VAL97
D	ALA98
D	LYS101
D	SER102
D	ARG106
D	LYS145
D	TYR175
D	HIS177
D	TYR180
D	LEU201
D	TYR240
D	ARG243
D	PHE247
D	PHE252
D	ASN282
D	HOH515
D	HOH772

---

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE COA B 404

Chain	Residue
B	GLY41
B	ILE42
B	VAL97
B	ALA98
B	LYS101
B	SER102
B	ARG106
B	LYS145
B	TYR175
B	HIS177
B	TYR180
B	LEU201
B	TYR240
B	ARG243
B	PHE247
B	PHE252
B	ASN282
B	HOH799
B	HOH803
B	HOH805
D	ARG38

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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