Tubulin polyglutamylase TTLL6
Intermolecular
Cysteine 259 and cysteine 179
Intramolecular
Cysteine 173 and cysteine 201
Cysteine 329 and cysteine 339
Cysteine 227 and cysteine 339
Cysteine 227 and cysteine 329
6vzt A 259 B 179
A redox-regulated disulphide may form between two units of Tubulin polyglutamylase TTLL6 at cysteines 259 and 179. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6vzt
Structure name
ttll6 bound to atp
Structure deposition date
2020-02-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
74
Peptide A name
Tubulin polyglutamylase TTLL6
Peptide B name
Tubulin polyglutamylase TTLL6
Peptide A accession
A4Q9E8
Peptide B accession
A4Q9E8
Peptide A residue number
259
Peptide B residue number
179
Ligandability
Cysteine 259 of Tubulin polyglutamylase TTLL6
Cysteine 179 of Tubulin polyglutamylase TTLL6
6vzw D 173 D 201
A redox-regulated disulphide may form within Tubulin polyglutamylase TTLL6 between cysteines 173 and 201. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
6vzw
Structure name
ttll6 bound to the initiation analog
Structure deposition date
2020-02-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
14
% buried
100
Peptide accession
A4Q9E8
Residue number A
173
Residue number B
201
Peptide name
Tubulin polyglutamylase TTLL6
Ligandability
Cysteine 173 of Tubulin polyglutamylase TTLL6
Cysteine 201 of Tubulin polyglutamylase TTLL6
6vzw A 329 A 339
A redox-regulated disulphide may form within Tubulin polyglutamylase TTLL6 between cysteines 329 and 339. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
6vzw
Structure name
ttll6 bound to the initiation analog
Structure deposition date
2020-02-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
60
Peptide accession
A4Q9E8
Residue number A
329
Residue number B
339
Peptide name
Tubulin polyglutamylase TTLL6
Ligandability
Cysteine 329 of Tubulin polyglutamylase TTLL6
Cysteine 339 of Tubulin polyglutamylase TTLL6
6vzw C 227 C 339
A redox-regulated disulphide may form within Tubulin polyglutamylase TTLL6 between cysteines 227 and 339. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6vzw
Structure name
ttll6 bound to the initiation analog
Structure deposition date
2020-02-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
94
Peptide accession
A4Q9E8
Residue number A
227
Residue number B
339
Peptide name
Tubulin polyglutamylase TTLL6
Ligandability
Cysteine 227 of Tubulin polyglutamylase TTLL6
Cysteine 339 of Tubulin polyglutamylase TTLL6
6vzw D 227 D 329
A redox-regulated disulphide may form within Tubulin polyglutamylase TTLL6 between cysteines 227 and 329. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6vzw
Structure name
ttll6 bound to the initiation analog
Structure deposition date
2020-02-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
54
Peptide accession
A4Q9E8
Residue number A
227
Residue number B
329
Peptide name
Tubulin polyglutamylase TTLL6
Ligandability
Cysteine 227 of Tubulin polyglutamylase TTLL6
Cysteine 329 of Tubulin polyglutamylase TTLL6
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