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3DGZ

Crystal Structure of Mouse Mitochondrial Thioredoxin Reductase, C-terminal 3-residue truncation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000305biological_processresponse to oxygen radical
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0007507biological_processheart development
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 Residues33
DetailsBINDING SITE FOR RESIDUE FAD A 500
ChainResidue
AGLY13
ACYS53
AVAL56
AGLY57
ACYS58
ALYS61
AILE124
AALA126
AALA154
ATHR155
AGLY156
AGLY15
ATYR195
AARG285
ALEU292
AGLY325
AASP326
AGLU333
ALEU334
ATHR335
APRO336
AHIS464
ASER16
AHOH511
AHOH513
AHOH515
AHOH611
AGLY17
AALA35
AASP36
ATYR37
AGLY51
ATHR52

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NA7 A 501
ChainResidue
AARG160
AGLY192
AALA193
ASER194
AARG216
ASER217
AARG221
AALA282
AILE283
AGLY284
AARG285
AGLU333
AHOH551
AHOH582
AHOH654

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP
ChainResidueDetails
AGLY50-PRO60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues29
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS58
ACYS53

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AGLU469
AHIS464

247947

PDB entries from 2026-01-21

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