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2JK6

Structure of Trypanothione Reductase from Leishmania infantum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004362molecular_functionglutathione-disulfide reductase (NADPH) activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006749biological_processglutathione metabolic process
A0015036molecular_functiondisulfide oxidoreductase activity
A0015042molecular_functiontrypanothione-disulfide reductase (NADPH) activity
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0034599biological_processcellular response to oxidative stress
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A0098869biological_processcellular oxidant detoxification
B0000166molecular_functionnucleotide binding
B0004362molecular_functionglutathione-disulfide reductase (NADPH) activity
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006749biological_processglutathione metabolic process
B0015036molecular_functiondisulfide oxidoreductase activity
B0015042molecular_functiontrypanothione-disulfide reductase (NADPH) activity
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0034599biological_processcellular response to oxidative stress
B0045454biological_processcell redox homeostasis
B0050660molecular_functionflavin adenine dinucleotide binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD A 1490
ChainResidue
AGLY11
ATHR51
ACYS52
AGLY56
ACYS57
ALYS60
AGLY127
AALA159
ATHR160
AGLY161
ATYR198
AGLY13
AARG287
AARG290
ALEU294
AGLY326
AASP327
AMET333
ALEU334
ATHR335
APRO336
BHIS461
ASER14
AGLY15
AVAL34
AASP35
AALA46
AALA47
AGLY50

site_idAC2
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD B 1490
ChainResidue
AHIS461
BGLY11
BGLY13
BSER14
BGLY15
BVAL34
BASP35
BALA46
BALA47
BGLY50
BTHR51
BCYS52
BCYS57
BLYS60
BGLY125
BGLY127
BALA159
BTHR160
BGLY161
BTYR198
BARG287
BARG290
BLEU294
BGLY326
BASP327
BMET333
BLEU334
BTHR335
BPRO336

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1491
ChainResidue
BTYR221
BARG222
BARG228

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1492
ChainResidue
BILE199
BALA284
BILE285
BGLY286
BARG287

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1491
ChainResidue
ATYR221
AARG222
AARG228

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1492
ChainResidue
AILE199
AALA284
AILE285
AGLY286
AARG287

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1493
ChainResidue
AGLN37
AALA38
ATHR39
AMET124

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP
ChainResidueDetails
AGLY49-PRO59

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS52
ACYS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BCYS52
BCYS57

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AGLU466
AHIS461

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BGLU466
BHIS461

224931

PDB entries from 2024-09-11

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