6PBR

Catalytic domain of E.coli dihydrolipoamide succinyltransferase in I4 space group

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004149	molecular_function	dihydrolipoyllysine-residue succinyltransferase activity
A	0006099	biological_process	tricarboxylic acid cycle
A	0016746	molecular_function	acyltransferase activity
A	0045252	cellular_component	oxoglutarate dehydrogenase complex
B	0004149	molecular_function	dihydrolipoyllysine-residue succinyltransferase activity
B	0006099	biological_process	tricarboxylic acid cycle
B	0016746	molecular_function	acyltransferase activity
B	0045252	cellular_component	oxoglutarate dehydrogenase complex
C	0004149	molecular_function	dihydrolipoyllysine-residue succinyltransferase activity
C	0006099	biological_process	tricarboxylic acid cycle
C	0016746	molecular_function	acyltransferase activity
C	0045252	cellular_component	oxoglutarate dehydrogenase complex
D	0004149	molecular_function	dihydrolipoyllysine-residue succinyltransferase activity
D	0006099	biological_process	tricarboxylic acid cycle
D	0016746	molecular_function	acyltransferase activity
D	0045252	cellular_component	oxoglutarate dehydrogenase complex
E	0004149	molecular_function	dihydrolipoyllysine-residue succinyltransferase activity
E	0006099	biological_process	tricarboxylic acid cycle
E	0016746	molecular_function	acyltransferase activity
E	0045252	cellular_component	oxoglutarate dehydrogenase complex
F	0004149	molecular_function	dihydrolipoyllysine-residue succinyltransferase activity
F	0006099	biological_process	tricarboxylic acid cycle
F	0016746	molecular_function	acyltransferase activity
F	0045252	cellular_component	oxoglutarate dehydrogenase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue NA A 501

Chain	Residue
A	LYS391
A	GLU395
B	LYS351

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site_id	AC2
Number of Residues	1
Details	binding site for residue NA B 501

Chain	Residue
B	GLU395

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site_id	AC3
Number of Residues	1
Details	binding site for residue NA D 501

Chain	Residue
D	GLU395

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site_id	AC4
Number of Residues	2
Details	binding site for residue NA E 501

Chain	Residue
E	GLU395
F	LYS351

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site_id	AC5
Number of Residues	2
Details	binding site for residue NA F 501

Chain	Residue
F	LYS391
F	GLU395

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"evidences":[{"source":"PubMed","id":"10739245","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9677295","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 704

Chain	Residue	Details
A	THR323	electrostatic stabiliser, polar interaction
A	HIS375	activator, proton acceptor, proton donor

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site_id	MCSA2
Number of Residues	2
Details	M-CSA 704

Chain	Residue	Details
B	THR323	electrostatic stabiliser, polar interaction
B	HIS375	activator, proton acceptor, proton donor

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site_id	MCSA3
Number of Residues	2
Details	M-CSA 704

Chain	Residue	Details
C	THR323	electrostatic stabiliser, polar interaction
C	HIS375	activator, proton acceptor, proton donor

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site_id	MCSA4
Number of Residues	2
Details	M-CSA 704

Chain	Residue	Details
D	THR323	electrostatic stabiliser, polar interaction
D	HIS375	activator, proton acceptor, proton donor

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site_id	MCSA5
Number of Residues	2
Details	M-CSA 704

Chain	Residue	Details
E	THR323	electrostatic stabiliser, polar interaction
E	HIS375	activator, proton acceptor, proton donor

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site_id	MCSA6
Number of Residues	2
Details	M-CSA 704

Chain	Residue	Details
F	THR323	electrostatic stabiliser, polar interaction
F	HIS375	activator, proton acceptor, proton donor

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