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4X43

Structure of proline-free E. coli Thioredoxin

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
Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGACKmIaaiL
ChainResidueDetails
ALEU24-LEU42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsSite: {"description":"Deprotonates C-terminal active site Cys"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsSite: {"description":"Contributes to redox potential value"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues107
DetailsDomain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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