1tde/1/1:A/2:A |
>1tde-a1-m1-cA (length=316) [Search sequence] |
GTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLT GPLLMERMHEHATKFETEIIFDHINKVDLQNRPFRLNGDNGEYTCDALIIATGASARYLG LPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGF RAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGLF VAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAG TGCMAALDAERYLDGL |
>1tde-a1-m2-cA (length=316) [Search sequence] |
GTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLT GPLLMERMHEHATKFETEIIFDHINKVDLQNRPFRLNGDNGEYTCDALIIATGASARYLG LPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGF RAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGLF VAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAG TGCMAALDAERYLDGL |
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PDB ID |
1tde (database links:
RCSB PDB
PDBe
PDBj
PDBsum) |
Title |
CRYSTAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN REDUCTASE REFINED AT 2 ANGSTROM RESOLUTION: IMPLICATIONS FOR A LARGE CONFORMATIONAL CHANGE DURING CATALYSIS |
Assembly ID |
1 |
Resolution |
2.1Å |
Method of structure determination |
X-RAY DIFFRACTION |
Number of inter-chain contacts |
166 |
Sequence identity between the two chains |
1.0 |
PubMed citation |
8114095 |
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Chain 1 |
Chain 2 |
Model ID |
1 |
2 |
Chain ID |
A |
A |
UniProt accession |
P0A9P4 |
P0A9P4 |
Species |
562 (Escherichia coli) |
562 (Escherichia coli) |
Function annotation |
BioLiP:1tdeA |
BioLiP:1tdeA |
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Switch viewer: [NGL] [JSmol]
Dimer structure:
Chain 1 in red;
Chain 2 in blue.
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Full biological assembly
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Other dimers with similar sequences and structures |
1cl0/1/1:A/2:A 1f6m/1/1:A/1:B 1f6m/2/1:E/1:F 1tdf/1/1:A/2:A 1trb/1/1:A/2:A |
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