ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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DCC-interacting protein 13-alpha

Intermolecular
Cysteine 570 and cysteine 570
Intramolecular
Cysteine 335 and cysteine 341
Cysteine 549 and cysteine 551
Cysteine 335 and cysteine 368
A redox-regulated disulphide may form between two units of DCC-interacting protein 13-alpha at cysteines 570 and 570. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2ela
Structure name
crystal structure of the ptb domain of human appl1
Structure deposition date
2007-03-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
40
Peptide A name
DCC-interacting protein 13-alpha
Peptide B name
DCC-interacting protein 13-alpha
Peptide A accession
Q9UKG1
Peptide B accession
Q9UKG1
Peptide A residue number
570
Peptide B residue number
570

Ligandability

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 DCC-interacting protein 13-alpha between cysteines 335 and 341.

Details

Redox score ?
65
PDB code
5c5b
Structure name
crystal structure of human appl bar-ph heterodimer
Structure deposition date
2015-06-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
36
Peptide accession
Q9UKG1
Residue number A
335
Residue number B
341
Peptide name
DCC-interacting protein 13-alpha

Ligandability

Cysteine 335 of DCC-interacting protein 13-alpha

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 341 of DCC-interacting protein 13-alpha

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 DCC-interacting protein 13-alpha between cysteines 549 and 551. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2ela
Structure name
crystal structure of the ptb domain of human appl1
Structure deposition date
2007-03-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
32
Peptide accession
Q9UKG1
Residue number A
549
Residue number B
551
Peptide name
DCC-interacting protein 13-alpha

Ligandability

Cysteine 549 of DCC-interacting protein 13-alpha

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 551 of DCC-interacting protein 13-alpha

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 DCC-interacting protein 13-alpha between cysteines 335 and 368. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2elb
Structure name
crystal structure of the bar-ph domain of human appl1
Structure deposition date
2007-03-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
18
Peptide accession
Q9UKG1
Residue number A
335
Residue number B
368
Peptide name
DCC-interacting protein 13-alpha

Ligandability

Cysteine 335 of DCC-interacting protein 13-alpha

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 368 of DCC-interacting protein 13-alpha

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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