8UGO

Structure of the complex between Human LIAS and H-protein in the presence of 5'-deoxyadenosine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006954	biological_process	inflammatory response
A	0006979	biological_process	response to oxidative stress
A	0009107	biological_process	lipoate biosynthetic process
A	0009249	biological_process	protein lipoylation
A	0016740	molecular_function	transferase activity
A	0016783	molecular_function	sulfurtransferase activity
A	0016992	molecular_function	lipoate synthase activity
A	0032496	biological_process	response to lipopolysaccharide
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006954	biological_process	inflammatory response
B	0006979	biological_process	response to oxidative stress
B	0009107	biological_process	lipoate biosynthetic process
B	0009249	biological_process	protein lipoylation
B	0016740	molecular_function	transferase activity
B	0016783	molecular_function	sulfurtransferase activity
B	0016992	molecular_function	lipoate synthase activity
B	0032496	biological_process	response to lipopolysaccharide
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005960	cellular_component	glycine cleavage complex
C	0019464	biological_process	glycine decarboxylation via glycine cleavage system
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006954	biological_process	inflammatory response
D	0006979	biological_process	response to oxidative stress
D	0009107	biological_process	lipoate biosynthetic process
D	0009249	biological_process	protein lipoylation
D	0016740	molecular_function	transferase activity
D	0016783	molecular_function	sulfurtransferase activity
D	0016992	molecular_function	lipoate synthase activity
D	0032496	biological_process	response to lipopolysaccharide
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0005515	molecular_function	protein binding
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0005960	cellular_component	glycine cleavage complex
E	0019464	biological_process	glycine decarboxylation via glycine cleavage system
F	0005515	molecular_function	protein binding
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0005960	cellular_component	glycine cleavage complex
F	0019464	biological_process	glycine decarboxylation via glycine cleavage system

Functional Information from PROSITE/UniProt

site_id	PS00189
Number of Residues	30
Details	LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GtkLnkqDEFgaLESvKAAseLysplsGeV

Chain	Residue	Details
E	GLY91-VAL120

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	657
Details	Domain: {"description":"Radical SAM core","evidences":[{"source":"PROSITE-ProRule","id":"PRU01266","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	21
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03123","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	164
Details	Domain: {"description":"Lipoyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	3
Details	Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1671321","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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