Ubiquitin carboxyl-terminal hydrolase 13

Intramolecular

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 13 between cysteines 211 and 214 (24 and 27 respectively in this structure).

Details

Redox score ?

PDB code

2l80

Structure name

solution structure of the zinc finger domain of usp13

Structure deposition date

2010-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q92995

Residue number A

211

Residue number B

214

Peptide name

Ubiquitin carboxyl-terminal hydrolase 13

Ligandability

Cysteine 211 of Ubiquitin carboxyl-terminal hydrolase 13

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 214 of Ubiquitin carboxyl-terminal hydrolase 13

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 13 between cysteines 214 and 231 (27 and 44 respectively in this structure).

Details

Redox score ?

PDB code

2l80

Structure name

solution structure of the zinc finger domain of usp13

Structure deposition date

2010-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q92995

Residue number A

214

Residue number B

231

Peptide name

Ubiquitin carboxyl-terminal hydrolase 13

Ligandability

Cysteine 214 of Ubiquitin carboxyl-terminal hydrolase 13

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 231 of Ubiquitin carboxyl-terminal hydrolase 13

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 13 between cysteines 211 and 231 (24 and 44 respectively in this structure).