Tubulin alpha chain
Intramolecular
Cysteine 315 and cysteine 316
Cysteine 315 and cysteine 347
Cysteine 4 and cysteine 129
Cysteine 295 and cysteine 376
Cysteine 295 and cysteine 315
Cysteine 316 and cysteine 376
Cysteine 200 and cysteine 316
Cysteine 315 and cysteine 376
5syg A 315 A 316
A redox-regulated disulphide may form within Tubulin alpha chain between cysteines 315 and 316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5syg
Structure name
cryo-em reconstruction of zampanolide-bound microtubule
Structure deposition date
2016-08-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
96
Peptide accession
B6A7R0
Residue number A
315
Residue number B
316
Peptide name
Tubulin alpha chain
Ligandability
Cysteine 315 of Tubulin alpha chain
Cysteine 316 of Tubulin alpha chain
5syc A 315 A 347
A redox-regulated disulphide may form within Tubulin alpha chain between cysteines 315 and 347. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5syc
Structure name
near-atomic resolution cryo-em reconstruction of peloruside-stabilized microtubule
Structure deposition date
2016-08-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
62
Peptide accession
B6A7R0
Residue number A
315
Residue number B
347
Peptide name
Tubulin alpha chain
Ligandability
Cysteine 315 of Tubulin alpha chain
Cysteine 347 of Tubulin alpha chain
5syc A 4 A 129
A redox-regulated disulphide may form within Tubulin alpha chain between cysteines 4 and 129. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5syc
Structure name
near-atomic resolution cryo-em reconstruction of peloruside-stabilized microtubule
Structure deposition date
2016-08-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
73
Peptide accession
B6A7R0
Residue number A
4
Residue number B
129
Peptide name
Tubulin alpha chain
Ligandability
Cysteine 4 of Tubulin alpha chain
Cysteine 129 of Tubulin alpha chain
5syg A 295 A 376
A redox-regulated disulphide may form within Tubulin alpha chain between cysteines 295 and 376. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
5syg
Structure name
cryo-em reconstruction of zampanolide-bound microtubule
Structure deposition date
2016-08-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
100
Peptide accession
B6A7R0
Residue number A
295
Residue number B
376
Peptide name
Tubulin alpha chain
Ligandability
Cysteine 295 of Tubulin alpha chain
Cysteine 376 of Tubulin alpha chain
5syc A 295 A 315
A redox-regulated disulphide may form within Tubulin alpha chain between cysteines 295 and 315. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
5syc
Structure name
near-atomic resolution cryo-em reconstruction of peloruside-stabilized microtubule
Structure deposition date
2016-08-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
B6A7R0
Residue number A
295
Residue number B
315
Peptide name
Tubulin alpha chain
Ligandability
Cysteine 295 of Tubulin alpha chain
Cysteine 315 of Tubulin alpha chain
5syg A 316 A 376
A redox-regulated disulphide may form within Tubulin alpha chain between cysteines 316 and 376. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
5syg
Structure name
cryo-em reconstruction of zampanolide-bound microtubule
Structure deposition date
2016-08-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
11
% buried
96
Peptide accession
B6A7R0
Residue number A
316
Residue number B
376
Peptide name
Tubulin alpha chain
Ligandability
Cysteine 316 of Tubulin alpha chain
Cysteine 376 of Tubulin alpha chain
5syf A 200 A 316
A redox-regulated disulphide may form within Tubulin alpha chain between cysteines 200 and 316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
5syf
Structure name
high-resolution cryo-em reconstruction of taxol-stabilized microtubule
Structure deposition date
2016-08-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
100
Peptide accession
B6A7R0
Residue number A
200
Residue number B
316
Peptide name
Tubulin alpha chain
Ligandability
Cysteine 200 of Tubulin alpha chain
Cysteine 316 of Tubulin alpha chain
5syf A 315 A 376
A redox-regulated disulphide may form within Tubulin alpha chain between cysteines 315 and 376. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
22
PDB code
5syf
Structure name
high-resolution cryo-em reconstruction of taxol-stabilized microtubule
Structure deposition date
2016-08-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
100
Peptide accession
B6A7R0
Residue number A
315
Residue number B
376
Peptide name
Tubulin alpha chain
Ligandability
Cysteine 315 of Tubulin alpha chain
Cysteine 376 of Tubulin alpha chain
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