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1ONF

Crystal structure of Plasmodium falciparum Glutathione reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004362molecular_functionglutathione-disulfide reductase (NADPH) activity
A0005737cellular_componentcytoplasm
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
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues30
DetailsBINDING SITE FOR RESIDUE FAD A 500
ChainResidue
AGLY8
AVAL42
AGLY43
ACYS44
ALYS47
AGLY108
ATHR109
AALA110
AALA147
AVAL148
AGLY149
AGLY9
ASER166
ATYR185
AARG272
AASP275
AGLY310
AASP311
AGLN351
ALEU352
ATHR353
APRO354
AGLY10
AHIS484
ASER11
AGLY12
AGLU31
ALYS32
ATHR38
ACYS39

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP
ChainResidueDetails
AGLY36-PRO46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
APRO485

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12729762, ECO:0007744|PDB:1ONF
ChainResidueDetails
AGLY12
ALYS32
ALYS48
ASER111
ACYS312
ALEU352

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AGLU489
AHIS484

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS44
ALYS47
ATYR185
AGLU189
ACYS39

223166

PDB entries from 2024-07-31

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