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4J57

Structure of Plasmodium falciparum thioredoxin reductase-thioredoxin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
B0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0045454biological_processcell redox homeostasis
B0050660molecular_functionflavin adenine dinucleotide binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0015035molecular_functionprotein-disulfide reductase activity
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0015035molecular_functionprotein-disulfide reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE FAD A 601
ChainResidue
AILE47
AGLY86
ATHR87
ACYS88
AVAL91
AGLY92
ACYS93
ALYS96
AGLY159
AALA161
AALA191
AGLY48
ATHR192
AGLY193
AARG316
AASP319
ALEU323
AGLY356
AASP357
AGLU364
ALEU365
AALA366
AGLY50
APRO367
AHOH701
AHOH704
AHOH711
BHIS509
APRO51
AGLY52
AASP71
ATYR72
AVAL73
ALYS74

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
ALYS58

site_idAC3
Number of Residues34
DetailsBINDING SITE FOR RESIDUE FAD B 600
ChainResidue
AHIS509
BGLY48
BGLY50
BPRO51
BGLY52
BASP71
BTYR72
BLYS74
BGLY86
BTHR87
BCYS88
BVAL91
BGLY92
BCYS93
BLYS96
BGLY159
BLEU160
BALA161
BALA191
BTHR192
BGLY193
BTYR232
BVAL233
BARG316
BASP319
BGLY356
BASP357
BGLU364
BLEU365
BALA366
BPRO367
BHOH701
BHOH702
BHOH704

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP
ChainResidueDetails
AGLY85-PRO95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P10599
ChainResidueDetails
ECYS30
ESER33
FCYS30
FSER33

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Deprotonates C-terminal active site Cys => ECO:0000305
ChainResidueDetails
EASP24
BTHR87
BGLY92
BALA161
BASP357
BGLU364
FASP24
ATHR87
AGLY92
AALA161
AASP357
AGLU364
BPRO51
BASP71

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Contributes to redox potential value => ECO:0000305
ChainResidueDetails
EGLY31
EPRO32
FGLY31
FPRO32

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PDB entries from 2025-06-11

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