1X2H

Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009249	biological_process	protein lipoylation
A	0016874	molecular_function	ligase activity
A	0016979	molecular_function	lipoate-protein ligase activity
A	0017118	molecular_function	lipoyltransferase activity
A	0036211	biological_process	protein modification process
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009249	biological_process	protein lipoylation
B	0016874	molecular_function	ligase activity
B	0016979	molecular_function	lipoate-protein ligase activity
B	0017118	molecular_function	lipoyltransferase activity
B	0036211	biological_process	protein modification process
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0009249	biological_process	protein lipoylation
C	0016874	molecular_function	ligase activity
C	0016979	molecular_function	lipoate-protein ligase activity
C	0017118	molecular_function	lipoyltransferase activity
C	0036211	biological_process	protein modification process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LPA A 338

Chain	Residue
A	GLU21
A	PHE24
A	SER72
A	ARG140
A	PHE147
A	HIS149

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LPA B 338

Chain	Residue
B	ALA138
B	ARG140
B	HIS149
B	LEU17
B	GLU21
B	PHE24

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	SER71
A	ALA76
A	VAL134
B	SER71
B	ALA76
B	VAL134
C	SER71
C	ALA76
C	VAL134

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