Transketolase
Intramolecular
Cysteine 41 and cysteine 42
Cysteine 362 and cysteine 386
Cysteine 362 and cysteine 376
Cysteine 376 and cysteine 386
Cysteine 133 and cysteine 151
Cysteine 413 and cysteine 417
Cysteine 133 and cysteine 362
Cysteine 133 and cysteine 376
Cysteine 386 and cysteine 413
4kxy A 41 A 42
A redox-regulated disulphide may form within Transketolase between cysteines 41 and 42. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
4kxy
Structure name
human transketolase in complex with thdp analogue (r)-2-(1,2- dihydroxyethyl)-3-deaza-thdp
Structure deposition date
2013-05-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
101
Minimum pKa ?
12
% buried
100
Peptide accession
P29401
Residue number A
41
Residue number B
42
Peptide name
Transketolase
Ligandability
Cysteine 41 of Transketolase
Cysteine 42 of Transketolase
6rjb B 362 B 386
A redox-regulated disulphide may form within Transketolase between cysteines 362 and 386. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
6rjb
Structure name
human transketolase variant t382e
Structure deposition date
2019-04-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
100
Minimum pKa ?
13
% buried
100
Peptide accession
P29401
Residue number A
362
Residue number B
386
Peptide name
Transketolase
Ligandability
Cysteine 362 of Transketolase
Cysteine 386 of Transketolase
4kxy A 362 A 376
A redox-regulated disulphide may form within Transketolase between cysteines 362 and 376. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
4kxy
Structure name
human transketolase in complex with thdp analogue (r)-2-(1,2- dihydroxyethyl)-3-deaza-thdp
Structure deposition date
2013-05-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
P29401
Residue number A
362
Residue number B
376
Peptide name
Transketolase
Ligandability
Cysteine 362 of Transketolase
Cysteine 376 of Transketolase
3ooy B 376 B 386
A redox-regulated disulphide may form within Transketolase between cysteines 376 and 386. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
3ooy
Structure name
crystal structure of human transketolase (tkt)
Structure deposition date
2010-08-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
102
Minimum pKa ?
12
% buried
100
Peptide accession
P29401
Residue number A
376
Residue number B
386
Peptide name
Transketolase
Ligandability
Cysteine 376 of Transketolase
Cysteine 386 of Transketolase
3ooy B 133 B 151
A redox-regulated disulphide may form within Transketolase between cysteines 133 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
3ooy
Structure name
crystal structure of human transketolase (tkt)
Structure deposition date
2010-08-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
97
Minimum pKa ?
13
% buried
100
Peptide accession
P29401
Residue number A
133
Residue number B
151
Peptide name
Transketolase
Ligandability
Cysteine 133 of Transketolase
Cysteine 151 of Transketolase
6ha3 A 413 A 417
A redox-regulated disulphide may form within Transketolase between cysteines 413 and 417. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
6ha3
Structure name
human transketolase variant e160q in covalent complex with donor ketose d-fructose-6-phosphate
Structure deposition date
2018-08-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
100
Minimum pKa ?
11
% buried
100
Peptide accession
P29401
Residue number A
413
Residue number B
417
Peptide name
Transketolase
Ligandability
Cysteine 413 of Transketolase
Cysteine 417 of Transketolase
6had A 133 A 362
A redox-regulated disulphide may form within Transketolase between cysteines 133 and 362. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
6had
Structure name
human transketolase variant e160q
Structure deposition date
2018-08-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
P29401
Residue number A
133
Residue number B
362
Peptide name
Transketolase
Ligandability
Cysteine 133 of Transketolase
Cysteine 362 of Transketolase
3ooy B 133 B 376
A redox-regulated disulphide may form within Transketolase between cysteines 133 and 376. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
3ooy
Structure name
crystal structure of human transketolase (tkt)
Structure deposition date
2010-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
97
Minimum pKa ?
12
% buried
100
Peptide accession
P29401
Residue number A
133
Residue number B
376
Peptide name
Transketolase
Ligandability
Cysteine 133 of Transketolase
Cysteine 376 of Transketolase
4kxu A 386 A 413
A redox-regulated disulphide may form within Transketolase between cysteines 386 and 413. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
22
PDB code
4kxu
Structure name
human transketolase in covalent complex with donor ketose d-fructose- 6-phosphate
Structure deposition date
2013-05-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
113
Minimum pKa ?
13
% buried
100
Peptide accession
P29401
Residue number A
386
Residue number B
413
Peptide name
Transketolase
Ligandability
Cysteine 386 of Transketolase
Cysteine 413 of Transketolase
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