Thioredoxin reductase 1, cytoplasmic
Intermolecular
Cysteine 647 and cysteine 32 of Thioredoxin L
Cysteine 608 and cysteine 608
Cysteine 497 and cysteine 59 L
Intramolecular
Cysteine 59 and cysteine 64 L
Cysteine 647 and cysteine 647
Cysteine 571 and cysteine 625
Cysteine 382 and cysteine 383 L
3qfa A 498 D 32
A redox-regulated disulphide may form between cysteine 647 of Thioredoxin reductase 1, cytoplasmic and cysteine 32 of Thioredoxin (498 and 32 respectively in this structure).
Details
Redox score ?
84
PDB code
3qfa
Structure name
crystal structure of the human thioredoxin reductase-thioredoxin complex
Structure deposition date
2011-01-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide A name
Thioredoxin reductase 1, cytoplasmic
Peptide B name
Thioredoxin
Peptide A accession
Q16881
Peptide B accession
P10599
Peptide A residue number
647
Peptide B residue number
32
Ligandability
Cysteine 647 of Thioredoxin reductase 1, cytoplasmic
Cysteine 32 of Thioredoxin
2zz0 C 458 D 458
A redox-regulated disulphide may form between two units of Thioredoxin reductase 1, cytoplasmic at cysteines 608 and 608 (458 and 458 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
2zz0
Structure name
crystal structure of human thioredoxin reductase i (secys 498 cys)
Structure deposition date
2009-02-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
75
Peptide A name
Thioredoxin reductase 1, cytoplasmic
Peptide B name
Thioredoxin reductase 1, cytoplasmic
Peptide A accession
Q16881
Peptide B accession
Q16881
Peptide A residue number
608
Peptide B residue number
608
Ligandability
1h6v E 497 F 59
A redox-regulated disulphide may form between two units of Thioredoxin reductase 1, cytoplasmic at cysteines 497 and 59. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
1h6v
Structure name
mammalian thioredoxin reductase
Structure deposition date
2001-06-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
13
% buried
nan
Peptide A name
Thioredoxin reductase 1, cytoplasmic
Peptide B name
Thioredoxin reductase 1, cytoplasmic
Peptide A accession
O89049
Peptide B accession
O89049
Peptide A residue number
497
Peptide B residue number
59
Ligandability
Cysteine 497 of Thioredoxin reductase 1, cytoplasmic
Cysteine 59 of Thioredoxin reductase 1, cytoplasmic
3eao E 59 E 64
A redox-regulated disulphide may form within Thioredoxin reductase 1, cytoplasmic between cysteines 59 and 64.
Details
Redox score ?
79
PDB code
3eao
Structure name
crystal structure of recombinant rat selenoprotein thioredoxin reductase 1 with oxidized c-terminal tail
Structure deposition date
2008-08-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
O89049
Residue number A
59
Residue number B
64
Peptide name
Thioredoxin reductase 1, cytoplasmic
Ligandability
Cysteine 59 of Thioredoxin reductase 1, cytoplasmic
Cysteine 64 of Thioredoxin reductase 1, cytoplasmic
2j3n D 497 D 498
A redox-regulated disulphide may form within Thioredoxin reductase 1, cytoplasmic between cysteines 647 and 647 (497 and 498 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2j3n
Structure name
x-ray structure of human thioredoxin reductase 1
Structure deposition date
2006-08-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
59
Peptide accession
Q16881
Residue number A
647
Residue number B
647
Peptide name
Thioredoxin reductase 1, cytoplasmic
Ligandability
Cysteine 647 of Thioredoxin reductase 1, cytoplasmic
Cysteine 647 of Thioredoxin reductase 1, cytoplasmic
2cfy A 421 A 475
A redox-regulated disulphide may form within Thioredoxin reductase 1, cytoplasmic between cysteines 571 and 625 (421 and 475 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2cfy
Structure name
crystal structure of human thioredoxin reductase 1
Structure deposition date
2006-02-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
100
Peptide accession
Q16881
Residue number A
571
Residue number B
625
Peptide name
Thioredoxin reductase 1, cytoplasmic
Ligandability
Cysteine 571 of Thioredoxin reductase 1, cytoplasmic
Cysteine 625 of Thioredoxin reductase 1, cytoplasmic
1h6v C 382 C 383
A redox-regulated disulphide may form within Thioredoxin reductase 1, cytoplasmic between cysteines 382 and 383. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
1h6v
Structure name
mammalian thioredoxin reductase
Structure deposition date
2001-06-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
O89049
Residue number A
382
Residue number B
383
Peptide name
Thioredoxin reductase 1, cytoplasmic
Ligandability
Cysteine 382 of Thioredoxin reductase 1, cytoplasmic
Cysteine 383 of Thioredoxin reductase 1, cytoplasmic
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