ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tubulin--tyrosine ligase

Intramolecular
Cysteine 338 and cysteine 347
Cysteine 91 and cysteine 294
Cysteine 72 and cysteine 294
A redox-regulated disulphide may form within Tubulin--tyrosine ligase between cysteines 338 and 347 (339 and 348 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
8asn
Structure name
crystal structure of the apo human ttl in complex with tubulin- stathmin
Structure deposition date
2022-08-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
75
Peptide accession
Q8NG68
Residue number A
338
Residue number B
347
Peptide name
Tubulin--tyrosine ligase

Ligandability

Cysteine 338 of Tubulin--tyrosine ligase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 347 of Tubulin--tyrosine ligase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Tubulin--tyrosine ligase between cysteines 91 and 294 (92 and 295 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
8asn
Structure name
crystal structure of the apo human ttl in complex with tubulin- stathmin
Structure deposition date
2022-08-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
100
Peptide accession
Q8NG68
Residue number A
91
Residue number B
294
Peptide name
Tubulin--tyrosine ligase

Ligandability

Cysteine 91 of Tubulin--tyrosine ligase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 294 of Tubulin--tyrosine ligase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Tubulin--tyrosine ligase between cysteines 72 and 294 (73 and 295 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
8asn
Structure name
crystal structure of the apo human ttl in complex with tubulin- stathmin
Structure deposition date
2022-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
100
Peptide accession
Q8NG68
Residue number A
72
Residue number B
294
Peptide name
Tubulin--tyrosine ligase

Ligandability

Cysteine 72 of Tubulin--tyrosine ligase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 294 of Tubulin--tyrosine ligase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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