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2FD3

Crystal Structure of Thioredoxin Mutant P34H

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0015035molecular_functionprotein-disulfide reductase activity
A0015036molecular_functiondisulfide oxidoreductase activity
A0030337molecular_functionDNA polymerase processivity factor activity
A0045454biological_processcell redox homeostasis
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0015035molecular_functionprotein-disulfide reductase activity
B0015036molecular_functiondisulfide oxidoreductase activity
B0030337molecular_functionDNA polymerase processivity factor activity
B0045454biological_processcell redox homeostasis
Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGHCKmIapiL
ChainResidueDetails
ALEU24-LEU42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AGLY33
ALYS36
BGLY33
BLYS36

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Deprotonates C-terminal active site Cys
ChainResidueDetails
APHE27
BPHE27

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Contributes to redox potential value
ChainResidueDetails
AHIS34
ACYS35
BHIS34
BCYS35

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ATYR70
BTYR70

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
AHIS34
ACYS35
ACYS32
AGLY33

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
BHIS34
BCYS35
BCYS32
BGLY33

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ACYS35
ACYS32

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
BCYS35
BCYS32

227344

PDB entries from 2024-11-13

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