ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Carboxypeptidase B2

Intramolecular
Cysteine 250 and cysteine 274
Cysteine 265 and cysteine 279
Cysteine 178 and cysteine 191
Cysteine 178 and cysteine 405
Cysteine 191 and cysteine 405
A redox-regulated disulphide may form within Carboxypeptidase B2 between cysteines 250 and 274 (228 and 252 respectively in this structure).

Details

Redox score ?
82
PDB code
7neu
Structure name
inhibitor complex with thrombin activatable fibrinolysis inhibitor (tafia)
Structure deposition date
2021-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96IY4
Residue number A
250
Residue number B
274
Peptide name
Carboxypeptidase B2

Ligandability

Cysteine 250 of Carboxypeptidase B2

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 274 of Carboxypeptidase B2

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 Carboxypeptidase B2 between cysteines 265 and 279 (243 and 257 respectively in this structure).

Details

Redox score ?
82
PDB code
5hvg
Structure name
crystal structure of thrombin-activatable fibrinolysis inhibitor in complex with an inhibitory nanobody (vhh-a204)
Structure deposition date
2016-01-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96IY4
Residue number A
265
Residue number B
279
Peptide name
Carboxypeptidase B2

Ligandability

Cysteine 265 of Carboxypeptidase B2

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 279 of Carboxypeptidase B2

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 Carboxypeptidase B2 between cysteines 178 and 191 (156 and 169 respectively in this structure).

Details

Redox score ?
77
PDB code
5hvg
Structure name
crystal structure of thrombin-activatable fibrinolysis inhibitor in complex with an inhibitory nanobody (vhh-a204)
Structure deposition date
2016-01-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96IY4
Residue number A
178
Residue number B
191
Peptide name
Carboxypeptidase B2

Ligandability

Cysteine 178 of Carboxypeptidase B2

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 191 of Carboxypeptidase B2

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 Carboxypeptidase B2 between cysteines 178 and 405. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4p10
Structure name
pro-carboxypeptidase u in complex with 5-(3-aminopropyl)-1-propyl-6,7- dihydro-4h-benzimidazole-5-carboxylic acid
Structure deposition date
2014-02-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
nan
Peptide accession
Q96IY4
Residue number A
178
Residue number B
405
Peptide name
Carboxypeptidase B2

Ligandability

Cysteine 178 of Carboxypeptidase B2

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 405 of Carboxypeptidase B2

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 Carboxypeptidase B2 between cysteines 191 and 405 (169 and 383 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3d67
Structure name
crystal structure of thrombin-activatable fibrinolysis inhibitor (tafi) in complex with 2-guanidino-ethyl-mercaptosuccinic acid (gemsa)
Structure deposition date
2008-05-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
nan
Peptide accession
Q96IY4
Residue number A
191
Residue number B
405
Peptide name
Carboxypeptidase B2

Ligandability

Cysteine 191 of Carboxypeptidase B2

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 405 of Carboxypeptidase B2

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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