Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1CL0

CRYSTAL STRUCTURE OF REDUCED THIOREDOXIN REDUCTASE FROM ESCHERICHIA COLI.

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
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A1902515cellular_componentthioredoxin-disulfide reductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD A 500
ChainResidue
AGLY12
AGLU38
AGLY41
AGLN42
ALEU43
ATHR46
AVAL49
AASN51
AHIS83
AILE84
AALA111
ASER13
ATHR112
AGLY113
ASER133
AALA134
ACYS138
AASN248
AGLY285
AASP286
AARG293
AGLN294
AGLY14
AALA295
ASER298
AHOH617
AHOH620
AHOH640
AHOH643
AHOH644
AHOH668
APRO15
AALA16
ATYR23
ATHR35
AGLY36
AMET37

Functional Information from PROSITE/UniProt
site_idPS00573
Number of Residues21
DetailsPYRIDINE_REDOX_2 Pyridine nucleotide-disulphide oxidoreductases class-II active site. CatCDGff..YrnqkVaVIGGGN
ChainResidueDetails
ACYS135-ASN155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8114095
ChainResidueDetails
AGLY36
AVAL287

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tde
ChainResidueDetails
ACYS135
ACYS138
AASP139

site_idMCSA1
Number of Residues3
DetailsM-CSA 381
ChainResidueDetails
AALA136covalent catalysis, proton shuttle (general acid/base)
AASP139covalent catalysis, proton shuttle (general acid/base)
AGLY140proton shuttle (general acid/base)

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon