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1DXL

Dihydrolipoamide dehydrogenase of glycine decarboxylase from Pisum Sativum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004148molecular_functiondihydrolipoyl dehydrogenase activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005960cellular_componentglycine cleavage complex
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0045252cellular_componentoxoglutarate dehydrogenase complex
A0050660molecular_functionflavin adenine dinucleotide binding
B0004148molecular_functiondihydrolipoyl dehydrogenase activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005960cellular_componentglycine cleavage complex
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0045252cellular_componentoxoglutarate dehydrogenase complex
B0050660molecular_functionflavin adenine dinucleotide binding
C0004148molecular_functiondihydrolipoyl dehydrogenase activity
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005960cellular_componentglycine cleavage complex
C0016491molecular_functionoxidoreductase activity
C0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
C0045252cellular_componentoxoglutarate dehydrogenase complex
C0050660molecular_functionflavin adenine dinucleotide binding
D0004148molecular_functiondihydrolipoyl dehydrogenase activity
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0005960cellular_componentglycine cleavage complex
D0016491molecular_functionoxidoreductase activity
D0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
D0045252cellular_componentoxoglutarate dehydrogenase complex
D0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues33
DetailsBINDING SITE FOR RESIDUE FAD A 480
ChainResidue
AILE12
ACYS45
AVAL48
AGLY49
ACYS50
ALYS54
AGLY116
ATYR117
AGLY118
AALA146
ATHR147
AGLY15
AGLY148
ASER149
ASER167
ATYR187
AILE188
AARG277
AASP317
AMET323
ALEU324
AALA325
APRO16
AHIS326
AALA328
ATYR356
BHIS449
AGLY17
AGLU36
ALYS37
AARG38
AGLY43
ATHR44

site_idAC2
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD B 480
ChainResidue
AHIS449
BILE12
BGLY15
BPRO16
BGLY17
BILE35
BGLU36
BLYS37
BARG38
BGLY43
BTHR44
BCYS45
BGLY49
BCYS50
BLYS54
BGLY116
BTYR117
BGLY118
BALA146
BTHR147
BGLY148
BSER149
BILE188
BARG277
BLEU284
BASP317
BMET323
BLEU324
BALA325
BHIS326
BALA328
BHOH2006

site_idAC3
Number of Residues33
DetailsBINDING SITE FOR RESIDUE FAD C 480
ChainResidue
CILE12
CGLY13
CGLY14
CGLY15
CPRO16
CGLY17
CGLU36
CLYS37
CARG38
CGLY43
CTHR44
CCYS45
CVAL48
CGLY49
CLYS54
CGLY116
CTYR117
CGLY118
CALA146
CTHR147
CGLY148
CILE188
CARG277
CPHE280
CASP317
CMET323
CLEU324
CALA325
CHIS326
CALA328
CTYR356
CHOH2001
DHIS449

site_idAC4
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD D 480
ChainResidue
DILE12
DGLY14
DGLY15
DPRO16
DGLY17
DILE35
DGLU36
DLYS37
DARG38
DGLY43
DTHR44
DCYS45
DGLY49
DCYS50
DLYS54
DGLY116
DTYR117
DGLY118
DALA146
DTHR147
DGLY148
DSER149
DILE188
DARG277
DASP317
DMET323
DLEU324
DALA325
DHIS326
DALA328
DTYR356
CHIS449

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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS449
BHIS449
CHIS449
DHIS449

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:10806386
ChainResidueDetails
AGLU36
CGLY118
CASP317
CMET323
DGLU36
DGLY118
DASP317
DMET323
AGLY118
AASP317
AMET323
BGLU36
BGLY118
BASP317
BMET323
CGLU36

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS54
BGLU207
BVAL241
BGLY276
CLYS54
CTHR147
CGLY184
CGLU207
CVAL241
CGLY276
DLYS54
ATHR147
DTHR147
DGLY184
DGLU207
DVAL241
DGLY276
AGLY184
AGLU207
AVAL241
AGLY276
BLYS54
BTHR147
BGLY184

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AGLU454
AHIS449

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BGLU454
BHIS449

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
CGLU454
CHIS449

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
DGLU454
DHIS449

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS45
ACYS50

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BCYS45
BCYS50

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
CCYS45
CCYS50

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
DCYS45
DCYS50

225946

PDB entries from 2024-10-09

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