8OHS

Core-binding domain of fungal E3-binding domain bound to the native pyruvate dehydrogenase E2 core

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004742	molecular_function	dihydrolipoyllysine-residue acetyltransferase activity
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
A	0006090	biological_process	pyruvate metabolic process
A	0016746	molecular_function	acyltransferase activity
A	0045254	cellular_component	pyruvate dehydrogenase complex
B	0004742	molecular_function	dihydrolipoyllysine-residue acetyltransferase activity
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
B	0006090	biological_process	pyruvate metabolic process
B	0016746	molecular_function	acyltransferase activity
B	0045254	cellular_component	pyruvate dehydrogenase complex
C	0004742	molecular_function	dihydrolipoyllysine-residue acetyltransferase activity
C	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
C	0016746	molecular_function	acyltransferase activity
C	0045254	cellular_component	pyruvate dehydrogenase complex
D	0004742	molecular_function	dihydrolipoyllysine-residue acetyltransferase activity
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
D	0006090	biological_process	pyruvate metabolic process
D	0016746	molecular_function	acyltransferase activity
D	0045254	cellular_component	pyruvate dehydrogenase complex
E	0004742	molecular_function	dihydrolipoyllysine-residue acetyltransferase activity
E	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
E	0016746	molecular_function	acyltransferase activity
E	0045254	cellular_component	pyruvate dehydrogenase complex
F	0004742	molecular_function	dihydrolipoyllysine-residue acetyltransferase activity
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
F	0006090	biological_process	pyruvate metabolic process
F	0016746	molecular_function	acyltransferase activity
F	0045254	cellular_component	pyruvate dehydrogenase complex
G	0004742	molecular_function	dihydrolipoyllysine-residue acetyltransferase activity
G	0005739	cellular_component	mitochondrion
G	0005759	cellular_component	mitochondrial matrix
G	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
G	0006090	biological_process	pyruvate metabolic process
G	0016746	molecular_function	acyltransferase activity
G	0045254	cellular_component	pyruvate dehydrogenase complex
H	0004742	molecular_function	dihydrolipoyllysine-residue acetyltransferase activity
H	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
H	0016746	molecular_function	acyltransferase activity
H	0045254	cellular_component	pyruvate dehydrogenase complex
I	0004742	molecular_function	dihydrolipoyllysine-residue acetyltransferase activity
I	0005739	cellular_component	mitochondrion
I	0005759	cellular_component	mitochondrial matrix
I	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
I	0006090	biological_process	pyruvate metabolic process
I	0016746	molecular_function	acyltransferase activity
I	0045254	cellular_component	pyruvate dehydrogenase complex

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	GLY56-MET85
A	GLY59-LEU88

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: ACT_SITE => ECO:0000255

Chain	Residue	Details
A	HIS431
G	ASP435
I	HIS431
I	ASP435
A	ASP435
B	HIS431
B	ASP435
D	HIS431
D	ASP435
F	HIS431
F	ASP435
G	HIS431

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N6-lipoyllysine => ECO:0000250, ECO:0000255|PROSITE-ProRule:PRU01066

Chain	Residue	Details
A	LYS75
B	LYS75
D	LYS75
F	LYS75
G	LYS75
I	LYS75

---