ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ubiquitin carboxyl-terminal hydrolase MINDY-2

Intermolecular
Cysteine 429 and cysteine 429
Cysteine 489 and cysteine 489
Intramolecular
Cysteine 385 and cysteine 397
A redox-regulated disulphide may form between two units of Ubiquitin carboxyl-terminal hydrolase MINDY-2 at cysteines 429 and 429.

Details

Redox score ?
65
PDB code
6z7v
Structure name
crystal structure of mindy2 (c266a) in complex with lys48 linked di- ubiquitin (k48-ub2)
Structure deposition date
2020-06-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
100
Peptide A name
Ubiquitin carboxyl-terminal hydrolase MINDY-2
Peptide B name
Ubiquitin carboxyl-terminal hydrolase MINDY-2
Peptide A accession
Q8NBR6
Peptide B accession
Q8NBR6
Peptide A residue number
429
Peptide B residue number
429

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 between two units of Ubiquitin carboxyl-terminal hydrolase MINDY-2 at cysteines 489 and 489. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7npi
Structure name
crystal structure of mindy2 (c266a) in complex with lys48-linked penta-ubiquitin (k48-ub5)
Structure deposition date
2021-02-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
13
% buried
96
Peptide A name
Ubiquitin carboxyl-terminal hydrolase MINDY-2
Peptide B name
Ubiquitin carboxyl-terminal hydrolase MINDY-2
Peptide A accession
Q8NBR6
Peptide B accession
Q8NBR6
Peptide A residue number
489
Peptide B residue number
489

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 Ubiquitin carboxyl-terminal hydrolase MINDY-2 between cysteines 385 and 397. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
7npi
Structure name
crystal structure of mindy2 (c266a) in complex with lys48-linked penta-ubiquitin (k48-ub5)
Structure deposition date
2021-02-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
35
Peptide accession
Q8NBR6
Residue number A
385
Residue number B
397
Peptide name
Ubiquitin carboxyl-terminal hydrolase MINDY-2

Ligandability

Cysteine 385 of Ubiquitin carboxyl-terminal hydrolase MINDY-2

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 397 of Ubiquitin carboxyl-terminal hydrolase MINDY-2

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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