7PSC

Crystal structure of the disease-causing I358T mutant of the human dihydrolipoamide dehydrogenase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001669	cellular_component	acrosomal vesicle
A	0004148	molecular_function	dihydrolipoyl dehydrogenase (NADH) activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005929	cellular_component	cilium
A	0006086	biological_process	pyruvate decarboxylation to acetyl-CoA
A	0006099	biological_process	tricarboxylic acid cycle
A	0006103	biological_process	2-oxoglutarate metabolic process
A	0009083	biological_process	branched-chain amino acid catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A	0019474	biological_process	L-lysine catabolic process to acetyl-CoA
A	0031410	cellular_component	cytoplasmic vesicle
A	0031514	cellular_component	motile cilium
A	0043159	cellular_component	acrosomal matrix
A	0045252	cellular_component	oxoglutarate dehydrogenase complex
A	0045254	cellular_component	pyruvate dehydrogenase complex
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0120551	biological_process	2-oxoglutarate decarboxylation to succinyl-CoA
A	0120552	biological_process	branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA
A	0160157	cellular_component	branched-chain alpha-ketoacid dehydrogenase complex
A	0160167	cellular_component	oxoadipate dehydrogenase complex
B	0001669	cellular_component	acrosomal vesicle
B	0004148	molecular_function	dihydrolipoyl dehydrogenase (NADH) activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005929	cellular_component	cilium
B	0006086	biological_process	pyruvate decarboxylation to acetyl-CoA
B	0006099	biological_process	tricarboxylic acid cycle
B	0006103	biological_process	2-oxoglutarate metabolic process
B	0009083	biological_process	branched-chain amino acid catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B	0019474	biological_process	L-lysine catabolic process to acetyl-CoA
B	0031410	cellular_component	cytoplasmic vesicle
B	0031514	cellular_component	motile cilium
B	0043159	cellular_component	acrosomal matrix
B	0045252	cellular_component	oxoglutarate dehydrogenase complex
B	0045254	cellular_component	pyruvate dehydrogenase complex
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0120551	biological_process	2-oxoglutarate decarboxylation to succinyl-CoA
B	0120552	biological_process	branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA
B	0160157	cellular_component	branched-chain alpha-ketoacid dehydrogenase complex
B	0160167	cellular_component	oxoadipate dehydrogenase complex

Functional Information from PROSITE/UniProt

site_id	PS00076
Number of Residues	11
Details	PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLnvGCIP

Chain	Residue	Details
A	GLY42-PRO52

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P09624","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	54
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15946682","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex","evidences":[{"source":"PubMed","id":"20385101","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	14
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	10
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6P6R2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---