Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2A87

Crystal Structure of M. tuberculosis Thioredoxin reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0015035molecular_functionprotein-disulfide reductase activity
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A0070402molecular_functionNADPH binding
B0001666biological_processresponse to hypoxia
B0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0015035molecular_functionprotein-disulfide reductase activity
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0045454biological_processcell redox homeostasis
B0050660molecular_functionflavin adenine dinucleotide binding
B0070402molecular_functionNADPH binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 336
ChainResidue
AHIS250
AARG295
ANAP381

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 336
ChainResidue
BHIS250
BARG295
BNAP481

site_idAC3
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD A 348
ChainResidue
APRO24
AALA25
APHE43
AGLU44
AGLY45
ASER47
AGLY49
AGLY50
AALA51
ALEU52
ATHR55
AVAL58
AGLU59
AASN60
AGLU91
AASP92
AVAL93
AALA121
AMET122
AGLY123
ACYS148
AASP149
AARG253
ALEU256
AGLY287
AASP288
AARG295
AGLN296
AALA297
AVAL298
AHOH385
AHOH387
BTYR32
AGLY21
ASER22
AGLY23

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAP A 381
ChainResidue
AARG127
ALEU129
AGLY164
AASP165
ASER166
AHIS185
AARG186
AARG187
AARG191
AILE248
AGLY249
APRO265
ATYR268
ALEU270
AARG292
AARG295
AMG336
BARG313

site_idAC5
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD B 448
ChainResidue
ATYR32
BILE20
BGLY21
BSER22
BPRO24
BALA25
BPHE43
BGLU44
BGLY45
BSER47
BPHE48
BGLY49
BGLY50
BALA51
BLEU52
BTHR55
BASN60
BVAL93
BMET122
BGLY123
BALA124
BCYS148
BASP149
BARG253
BLEU256
BGLY287
BASP288
BARG295
BGLN296
BALA297
BVAL298

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAP B 481
ChainResidue
BARG186
BARG191
BALA247
BILE248
BGLY249
BGLU251
BTYR268
BARG292
BARG295
BMG336
BILE161
BGLY162
BGLY163
BGLY164
BASP165
BSER166
BGLU169
BHIS185

Functional Information from PROSITE/UniProt
site_idPS00573
Number of Residues21
DetailsPYRIDINE_REDOX_2 Pyridine nucleotide-disulphide oxidoreductases class-II active site. CatCDGff..FrdqdIaVIGGGD
ChainResidueDetails
ACYS145-ASP165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsBINDING: BINDING => ECO:0000269|PubMed:16301794, ECO:0007744|PDB:2A87
ChainResidueDetails
ASER22
AASP288
AARG295
BSER22
BGLU44
BASN60
BVAL93
BSER166
BHIS185
BARG191
BILE248
AGLU44
BTYR268
BASP288
BARG295
AASN60
AVAL93
ASER166
AHIS185
AARG191
AILE248
ATYR268

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609
ChainResidueDetails
ATHR2
BTHR2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by PtkA => ECO:0000269|PubMed:29317718
ChainResidueDetails
ATYR32
BTYR32

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tde
ChainResidueDetails
ACYS145
ACYS148
AASP149

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tde
ChainResidueDetails
BCYS145
BCYS148
BASP149

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon