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7PSC

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0001669cellular_componentacrosomal vesicle
A0004148molecular_functiondihydrolipoyl dehydrogenase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005929cellular_componentcilium
A0005967cellular_componentobsolete mitochondrial pyruvate dehydrogenase complex
A0006086biological_processacetyl-CoA biosynthetic process from pyruvate
A0006120biological_processmitochondrial electron transport, NADH to ubiquinone
A0006508biological_processproteolysis
A0007369biological_processgastrulation
A0009083biological_processbranched-chain amino acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0031410cellular_componentcytoplasmic vesicle
A0031514cellular_componentmotile cilium
A0034604molecular_functionpyruvate dehydrogenase (NAD+) activity
A0042391biological_processregulation of membrane potential
A0043159cellular_componentacrosomal matrix
A0045240cellular_componentalpha-ketoacid dehydrogenase complex
A0045252cellular_componentoxoglutarate dehydrogenase complex
A0045254cellular_componentpyruvate dehydrogenase complex
A0047101molecular_functionbranched-chain alpha-keto acid dehydrogenase activity
A0048240biological_processsperm capacitation
A0050660molecular_functionflavin adenine dinucleotide binding
A1902493cellular_componentacetyltransferase complex
B0001669cellular_componentacrosomal vesicle
B0004148molecular_functiondihydrolipoyl dehydrogenase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005929cellular_componentcilium
B0005967cellular_componentobsolete mitochondrial pyruvate dehydrogenase complex
B0006086biological_processacetyl-CoA biosynthetic process from pyruvate
B0006120biological_processmitochondrial electron transport, NADH to ubiquinone
B0006508biological_processproteolysis
B0007369biological_processgastrulation
B0009083biological_processbranched-chain amino acid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0031410cellular_componentcytoplasmic vesicle
B0031514cellular_componentmotile cilium
B0034604molecular_functionpyruvate dehydrogenase (NAD+) activity
B0042391biological_processregulation of membrane potential
B0043159cellular_componentacrosomal matrix
B0045240cellular_componentalpha-ketoacid dehydrogenase complex
B0045252cellular_componentoxoglutarate dehydrogenase complex
B0045254cellular_componentpyruvate dehydrogenase complex
B0047101molecular_functionbranched-chain alpha-keto acid dehydrogenase activity
B0048240biological_processsperm capacitation
B0050660molecular_functionflavin adenine dinucleotide binding
B1902493cellular_componentacetyltransferase complex
Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLnvGCIP
ChainResidueDetails
AGLY42-PRO52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P09624
ChainResidueDetails
AHIS452
BHIS452

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:15946682
ChainResidueDetails
AGLU36
AMET326
BGLU36
BLYS54
BGLY119
BTHR148
BGLY185
BGLU208
BVAL243
BGLY279
BASP320
ALYS54
BMET326
AGLY119
ATHR148
AGLY185
AGLU208
AVAL243
AGLY279
AASP320

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex => ECO:0000269|PubMed:20385101
ChainResidueDetails
AASP413
ATYR438
BASP413
BTYR438

site_idSWS_FT_FI4
Number of Residues14
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:O08749
ChainResidueDetails
ALYS31
BLYS87
BLYS97
BLYS108
BLYS375
BLYS470
ALYS69
ALYS87
ALYS97
ALYS108
ALYS375
ALYS470
BLYS31
BLYS69

site_idSWS_FT_FI5
Number of Residues10
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O08749
ChainResidueDetails
ALYS124
BLYS395
ALYS131
ALYS238
ALYS242
ALYS395
BLYS124
BLYS131
BLYS238
BLYS242

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08749
ChainResidueDetails
ASER250
BSER250

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6P6R2
ChainResidueDetails
ASER262
BSER262

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O08749
ChainResidueDetails
ALYS311
ALYS385
BLYS311
BLYS385

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS382
BLYS382

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER467
BSER467

222036

PDB entries from 2024-07-03

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