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2EIO

Design of Disulfide-linked Thioredoxin Dimers and Multimers Through Analysis of Crystal Contacts

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0015035molecular_functionprotein-disulfide reductase activity
A0030337molecular_functionDNA polymerase processivity factor activity
A0045454biological_processcell redox homeostasis
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0015035molecular_functionprotein-disulfide reductase activity
B0030337molecular_functionDNA polymerase processivity factor activity
B0045454biological_processcell redox homeostasis
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0015035molecular_functionprotein-disulfide reductase activity
C0030337molecular_functionDNA polymerase processivity factor activity
C0045454biological_processcell redox homeostasis
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0015035molecular_functionprotein-disulfide reductase activity
D0030337molecular_functionDNA polymerase processivity factor activity
D0045454biological_processcell redox homeostasis
Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGPCKmIapiL
ChainResidueDetails
ALEU24-LEU42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsSite: {"description":"Deprotonates C-terminal active site Cys"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsSite: {"description":"Contributes to redox potential value"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
APRO34
ACYS35
ACYS32
AGLY33

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
BPRO34
BCYS35
BCYS32
BGLY33

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
CPRO34
CCYS35
CCYS32
CGLY33

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
DPRO34
DCYS35
DCYS32
DGLY33

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ACYS35
ACYS32

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
BCYS35
BCYS32

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
CCYS35
CCYS32

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
DCYS35
DCYS32

243531

PDB entries from 2025-10-22

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