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2A8X

Crystal Structure of Lipoamide Dehydrogenase from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004148molecular_functiondihydrolipoyl dehydrogenase activity
A0004591molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0015036molecular_functiondisulfide oxidoreductase activity
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0035375molecular_functionzymogen binding
A0045254cellular_componentpyruvate dehydrogenase complex
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A0070404molecular_functionNADH binding
A0098869biological_processcellular oxidant detoxification
B0004148molecular_functiondihydrolipoyl dehydrogenase activity
B0004591molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0015036molecular_functiondisulfide oxidoreductase activity
B0016209molecular_functionantioxidant activity
B0016491molecular_functionoxidoreductase activity
B0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0035375molecular_functionzymogen binding
B0045254cellular_componentpyruvate dehydrogenase complex
B0045454biological_processcell redox homeostasis
B0050660molecular_functionflavin adenine dinucleotide binding
B0070404molecular_functionNADH binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD A 480
ChainResidue
ALEU9
AGLY39
AVAL40
ACYS41
AGLY45
ACYS46
ALYS50
ATYR112
AGLY113
AALA141
ATHR142
AGLY10
AGLY143
ATYR161
AILE182
ATYR276
AGLY308
AASP309
AGLN315
ALEU316
AALA317
AHIS318
AGLY12
AHOH591
AHOH594
AHOH599
AHOH609
AHOH658
AHOH729
BHIS443
BPRO444
APRO13
AGLY14
AVAL32
AGLU33
APRO34
ATYR36

site_idAC2
Number of Residues38
DetailsBINDING SITE FOR RESIDUE FAD B 580
ChainResidue
AHIS443
APRO444
BLEU9
BGLY10
BGLY12
BPRO13
BGLY14
BVAL32
BGLU33
BPRO34
BTYR36
BGLY39
BVAL40
BCYS41
BGLY45
BCYS46
BLYS50
BTYR112
BGLY113
BALA141
BTHR142
BGLY143
BTYR161
BILE182
BTYR276
BGLY308
BASP309
BGLN315
BLEU316
BALA317
BHIS318
BPHE350
BHOH583
BHOH604
BHOH630
BHOH635
BHOH657
BHOH702

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 590
ChainResidue
ATYR16
AARG93
AGLY96
ALEU100
BALA381
BASN463

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGvCLnvGCIP
ChainResidueDetails
AGLY38-PRO48

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS443
BHIS443

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16093239, ECO:0000269|PubMed:20078138
ChainResidueDetails
AGLU33
ALYS50
AASP309
AALA317
BGLU33
BLYS50
BASP309
BALA317

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY113
AGLY178
AGLU201
AALA266
BGLY113
BGLY178
BGLU201
BALA266

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS46
ACYS41

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BCYS46
BCYS41

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AHIS443
AGLU448

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BHIS443
BGLU448

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PDB entries from 2024-10-30

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