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1ZKQ

Crystal structure of mouse thioredoxin reductase type 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000305biological_processresponse to oxygen radical
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0007507biological_processheart development
A0010035biological_processobsolete response to inorganic substance
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0030097biological_processhemopoiesis
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0042803molecular_functionprotein homodimerization activity
A0043025cellular_componentneuronal cell body
A0044877molecular_functionprotein-containing complex binding
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 600
ChainResidue
AGLY46
ALYS94
ALYS158
AALA159
AALA187
ATHR188
AGLY189
ASER208
ATYR228
AVAL229
AARG318
ASER49
ATHR324
ALEU325
AGLY358
AASP359
AGLU366
ALEU367
ATHR368
APRO369
APHE400
AHIS497
AGLY50
AHOH605
AHOH617
AHOH622
AASP69
ATYR70
AGLY84
ATHR85
ACYS86
ACYS91

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP
ChainResidueDetails
AGLY83-PRO93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS497

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP41

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS79
ALYS175
ALYS329

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Cysteinyl-selenocysteine (Cys-Sec) => ECO:0000250
ChainResidueDetails
ACYS522
ACYS523

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS86
ACYS91

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AHIS497
AGLU502

222036

PDB entries from 2024-07-03

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