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1TRB

CONVERGENT EVOLUTION OF SIMILAR FUNCTION IN TWO STRUCTURALLY DIVERGENT ENZYMES

Functional Information from GO Data
ChainGOidnamespacecontents
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0032991cellular_componentprotein-containing complex
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A1902515cellular_componentthioredoxin-disulfide reductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues38
DetailsBINDING SITE FOR RESIDUE FAD A 500
ChainResidue
AGLY12
AGLU38
AGLY41
AGLN42
ALEU43
ATHR46
AVAL49
AASN51
AHIS83
AILE84
AALA111
ASER13
ATHR112
AGLY113
ATYR118
ASER138
AGLY285
AASP286
AARG293
AGLN294
AALA295
ASER298
AGLY14
AHOH602
AHOH605
AHOH607
AHOH613
AHOH615
AHOH617
AHOH623
AHOH675
AHOH767
APRO15
AALA16
ATYR23
ATHR35
AGLY36
AMET37

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8114095","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tde
ChainResidueDetails
ACYS135
ASER138
AASP139

site_idMCSA1
Number of Residues3
DetailsM-CSA 381
ChainResidueDetails
ACYS135covalent catalysis, proton shuttle (general acid/base)
ASER138covalent catalysis, proton shuttle (general acid/base)
AASP139proton shuttle (general acid/base)

246031

PDB entries from 2025-12-10

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