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3F3Q

Crystal structure of the oxidised form of thioredoxin 1 from saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000011biological_processvacuole inheritance
A0000139cellular_componentGolgi membrane
A0000324cellular_componentfungal-type vacuole
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
A0006890biological_processretrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0015031biological_processprotein transport
A0015035molecular_functionprotein-disulfide reductase activity
A0015036molecular_functiondisulfide oxidoreductase activity
A0016020cellular_componentmembrane
A0042144biological_processvacuole fusion, non-autophagic
A0045454biological_processcell redox homeostasis
A0120124cellular_componentmembrane fusion priming complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 104
ChainResidue
AHIS-1
AHIS-4
AGLU45
AHOH158

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 105
ChainResidue
AHIS-2
AHIS0
AGLU68
AHOH136

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 106
ChainResidue
AHIS-3
AASP12
AHOH181
AHIS-5

Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. VVdFYatWCGPCKmIapmI
ChainResidueDetails
AVAL22-ILE40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues101
DetailsDomain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Deprotonates C-terminal active site Cys"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Contributes to redox potential value"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
AGLY31
ACYS30
APRO32
ACYS33

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ACYS30
ACYS33

238895

PDB entries from 2025-07-16

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