ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ubiquitin carboxyl-terminal hydrolase CYLD

Intramolecular
Cysteine 507 and cysteine 510
Cysteine 510 and cysteine 523
Cysteine 507 and cysteine 523
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 507 and 510 (510 and 513 respectively in this structure).

Details

Redox score ?
83
PDB code
7owc
Structure name
structure of cyld cap-gly3 (467-565) bound to ub; orthorhobic space group
Structure deposition date
2021-06-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
7
Peptide accession
J3KRR7
Residue number A
507
Residue number B
510
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD

Ligandability

Cysteine 507 of Ubiquitin carboxyl-terminal hydrolase CYLD

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 510 of Ubiquitin carboxyl-terminal hydrolase CYLD

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 Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 510 and 523 (513 and 526 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
7owc
Structure name
structure of cyld cap-gly3 (467-565) bound to ub; orthorhobic space group
Structure deposition date
2021-06-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
11
% buried
nan
Peptide accession
J3KRR7
Residue number A
510
Residue number B
523
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD

Ligandability

Cysteine 510 of Ubiquitin carboxyl-terminal hydrolase CYLD

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 523 of Ubiquitin carboxyl-terminal hydrolase CYLD

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 Ubiquitin carboxyl-terminal hydrolase CYLD between cysteines 507 and 523 (510 and 526 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
7owc
Structure name
structure of cyld cap-gly3 (467-565) bound to ub; orthorhobic space group
Structure deposition date
2021-06-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
47
Minimum pKa ?
11
% buried
nan
Peptide accession
J3KRR7
Residue number A
507
Residue number B
523
Peptide name
Ubiquitin carboxyl-terminal hydrolase CYLD

Ligandability

Cysteine 507 of Ubiquitin carboxyl-terminal hydrolase CYLD

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 523 of Ubiquitin carboxyl-terminal hydrolase CYLD

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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