ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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TBC1 domain family member 15

Intramolecular
Cysteine 575 and cysteine 583
Cysteine 486 and cysteine 524
Cysteine 524 and cysteine 525
Cysteine 472 and cysteine 525
Cysteine 486 and cysteine 525
A redox-regulated disulphide may form within TBC1 domain family member 15 between cysteines 575 and 583 (600 and 608 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
5tuc
Structure name
crystal structure of the sus tbc1d15 gap domain
Structure deposition date
2016-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
0
Peptide accession
F1SH24
Residue number A
575
Residue number B
583
Peptide name
TBC1 domain family member 15

Ligandability

Cysteine 575 of TBC1 domain family member 15

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 583 of TBC1 domain family member 15

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 TBC1 domain family member 15 between cysteines 486 and 524 (511 and 549 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5tuc
Structure name
crystal structure of the sus tbc1d15 gap domain
Structure deposition date
2016-11-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
100
Peptide accession
F1SH24
Residue number A
486
Residue number B
524
Peptide name
TBC1 domain family member 15

Ligandability

Cysteine 486 of TBC1 domain family member 15

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 524 of TBC1 domain family member 15

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 TBC1 domain family member 15 between cysteines 524 and 525 (549 and 550 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5tuc
Structure name
crystal structure of the sus tbc1d15 gap domain
Structure deposition date
2016-11-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
100
Peptide accession
F1SH24
Residue number A
524
Residue number B
525
Peptide name
TBC1 domain family member 15

Ligandability

Cysteine 524 of TBC1 domain family member 15

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 525 of TBC1 domain family member 15

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 TBC1 domain family member 15 between cysteines 472 and 525 (497 and 550 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
5tuc
Structure name
crystal structure of the sus tbc1d15 gap domain
Structure deposition date
2016-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
78
Peptide accession
F1SH24
Residue number A
472
Residue number B
525
Peptide name
TBC1 domain family member 15

Ligandability

Cysteine 472 of TBC1 domain family member 15

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 525 of TBC1 domain family member 15

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 TBC1 domain family member 15 between cysteines 486 and 525 (511 and 550 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
5tuc
Structure name
crystal structure of the sus tbc1d15 gap domain
Structure deposition date
2016-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
100
Peptide accession
F1SH24
Residue number A
486
Residue number B
525
Peptide name
TBC1 domain family member 15

Ligandability

Cysteine 486 of TBC1 domain family member 15

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 525 of TBC1 domain family member 15

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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