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1EBD

DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004148molecular_functiondihydrolipoyl dehydrogenase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0050660molecular_functionflavin adenine dinucleotide binding
B0004148molecular_functiondihydrolipoyl dehydrogenase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0050660molecular_functionflavin adenine dinucleotide binding
C0016746molecular_functionacyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 462
ChainResidue
AGLY16
ACYS47
AVAL50
AGLY51
ACYS52
ALYS56
AGLY117
AGLU118
AALA119
AALA146
ATHR147
AGLY18
AGLY148
ATYR186
AILE187
AARG274
AGLY313
AASP314
AALA320
ALEU321
AALA322
AHOH470
APRO19
AHOH478
BHIS446
BPRO447
AGLY20
AVAL38
AGLU39
ALYS40
AGLY45
AVAL46

site_idAC2
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD B 462
ChainResidue
AHIS446
APRO447
BGLY16
BGLY18
BPRO19
BGLY20
BGLU39
BLYS40
BGLY45
BVAL46
BCYS47
BCYS52
BLYS56
BGLY117
BGLU118
BALA119
BALA146
BTHR147
BGLY148
BTYR186
BILE187
BARG274
BGLY313
BASP314
BALA320
BLEU321
BALA322
BHOH463
BHOH478

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGvCLnvGCIP
ChainResidueDetails
AGLY44-PRO54

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS446
BHIS446

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:8805537
ChainResidueDetails
AGLU39
ALYS56
AASP314
AALA322
BGLU39
BLYS56
BASP314
BALA322

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AALA119
AGLY183
AGLU206
ATHR271
BALA119
BGLY183
BGLU206
BTHR271

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AGLU451
AHIS446

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BGLU451
BHIS446

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS47
ACYS52

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BCYS47
BCYS52

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PDB entries from 2024-05-01

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