ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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NCK-interacting protein with SH3 domain

Intramolecular
Cysteine 429 and cysteine 433
Cysteine 376 and cysteine 429
Cysteine 502 and cysteine 554
Cysteine 433 and cysteine 463
A redox-regulated disulphide may form within NCK-interacting protein with SH3 domain between cysteines 429 and 433. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6dee
Structure name
crystal structure of the c-terminus of homo sapiens spin90 (sh3- protein interacting with nck), residues 306-722
Structure deposition date
2018-05-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
72
Peptide accession
Q9NZQ3
Residue number A
429
Residue number B
433
Peptide name
NCK-interacting protein with SH3 domain

Ligandability

Cysteine 429 of NCK-interacting protein with SH3 domain

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 433 of NCK-interacting protein with SH3 domain

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 NCK-interacting protein with SH3 domain between cysteines 376 and 429. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6dee
Structure name
crystal structure of the c-terminus of homo sapiens spin90 (sh3- protein interacting with nck), residues 306-722
Structure deposition date
2018-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
46
Peptide accession
Q9NZQ3
Residue number A
376
Residue number B
429
Peptide name
NCK-interacting protein with SH3 domain

Ligandability

Cysteine 376 of NCK-interacting protein with SH3 domain

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 429 of NCK-interacting protein with SH3 domain

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 NCK-interacting protein with SH3 domain between cysteines 502 and 554. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6ded
Structure name
crystal structure of the c-terminal arm domain of homo sapiens spin90 (sh3-protein interacting with nck), residues 351-722
Structure deposition date
2018-05-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
64
Peptide accession
Q9NZQ3
Residue number A
502
Residue number B
554
Peptide name
NCK-interacting protein with SH3 domain

Ligandability

Cysteine 502 of NCK-interacting protein with SH3 domain

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 554 of NCK-interacting protein with SH3 domain

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 NCK-interacting protein with SH3 domain between cysteines 433 and 463. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
6ded
Structure name
crystal structure of the c-terminal arm domain of homo sapiens spin90 (sh3-protein interacting with nck), residues 351-722
Structure deposition date
2018-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
94
Peptide accession
Q9NZQ3
Residue number A
433
Residue number B
463
Peptide name
NCK-interacting protein with SH3 domain

Ligandability

Cysteine 433 of NCK-interacting protein with SH3 domain

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 463 of NCK-interacting protein with SH3 domain

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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