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3PIN

Crystal structure of Mxr1 from Saccharomyces cerevisiae in complex with Trx2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000011biological_processvacuole inheritance
A0000103biological_processsulfate assimilation
A0000139cellular_componentGolgi membrane
A0000324cellular_componentfungal-type vacuole
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006749biological_processglutathione metabolic process
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
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0008113molecular_functionpeptide-methionine (S)-S-oxide reductase activity
B0016491molecular_functionoxidoreductase activity
B0016671molecular_functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
B0033744molecular_functionL-methionine:thioredoxin-disulfide S-oxidoreductase activity
B0034599biological_processcellular response to oxidative stress
B0036456molecular_functionL-methionine-(S)-S-oxide reductase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
BSER58
ASER34

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Deprotonates C-terminal active site Cys
ChainResidueDetails
AASP25

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Contributes to redox potential value
ChainResidueDetails
AGLY32
APRO33

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER62

site_idSWS_FT_FI5
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS67
ALYS97

237735

PDB entries from 2025-06-18

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