a tool for identifying drug-targetable redox-active disulphides

Angiotensin-converting enzyme 2

Intermolecular

Cysteine 141 and cysteine 141

Cysteine 133 and cysteine 133

Intramolecular

Cysteine 133 and cysteine 141

Cysteine 530 and cysteine 542

Cysteine 344 and cysteine 361

A redox-regulated disulphide may form between two units of Angiotensin-converting enzyme 2 at cysteines 141 and 141. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

56

PDB code

Structure name

ace2 -targeting monoclonal antibody as potent and broad-spectrum coronavirus blocker

Structure deposition date

2021-08-18

Thiol separation (Å)

7

Half-sphere exposure sum ?

52

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Angiotensin-converting enzyme 2

Peptide B name

Angiotensin-converting enzyme 2

Peptide A accession

Peptide B accession

Peptide A residue number

141

Peptide B residue number

141

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 Angiotensin-converting enzyme 2 at cysteines 133 and 133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

47

PDB code

Structure name

sit1-ace2-ba

Structure deposition date

2022-06-21

Thiol separation (Å)

8

Half-sphere exposure sum ?

52

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Angiotensin-converting enzyme 2

Peptide B name

Angiotensin-converting enzyme 2

Peptide A accession

Peptide B accession

Peptide A residue number

133

Peptide B residue number

133

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 Angiotensin-converting enzyme 2 between cysteines 133 and 141.

Details

Redox score ?

80

PDB code

Structure name

the co-crystal structure of ace2 with fab

Structure deposition date

2021-02-26

Thiol separation (Å)

4

Half-sphere exposure sum ?

45

Minimum pK_a ?

9

% buried

0

Peptide accession

Residue number A

133

Residue number B

141

Peptide name

Angiotensin-converting enzyme 2

Ligandability

Cysteine 133 of Angiotensin-converting enzyme 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 141 of Angiotensin-converting enzyme 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.

A redox-regulated disulphide may form within Angiotensin-converting enzyme 2 between cysteines 530 and 542.

Details

Redox score ?

78

PDB code

Structure name

crystal structure of affinity-enhancing and catalytically inactive ace2 in complex with sars-cov-2 rbd

Structure deposition date

2021-08-04

Thiol separation (Å)

3

Half-sphere exposure sum ?

68

Minimum pK_a ?

7

% buried

68

Peptide accession

Residue number A

530

Residue number B

542

Peptide name

Angiotensin-converting enzyme 2

Ligandability

Cysteine 530 of Angiotensin-converting enzyme 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 542 of Angiotensin-converting enzyme 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.

A redox-regulated disulphide may form within Angiotensin-converting enzyme 2 between cysteines 344 and 361.

Details

Redox score ?

68

PDB code

Structure name

the co-crystal structure of ace2 with fab

Structure deposition date

2021-02-26

Thiol separation (Å)

4

Half-sphere exposure sum ?

75

Minimum pK_a ?

9

% buried

90

Peptide accession

Residue number A

344

Residue number B

361

Peptide name

Angiotensin-converting enzyme 2

Ligandability

Cysteine 344 of Angiotensin-converting enzyme 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 361 of Angiotensin-converting enzyme 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.

If this tool was useful for finding a disulphide, please cite: