a tool for identifying drug-targetable redox-active disulphides

Sterol O-acyltransferase 1

Intramolecular

Cysteine 528 and cysteine 546

Cysteine 365 and cysteine 516

Cysteine 333 and cysteine 387

Cysteine 345 and cysteine 365

Cysteine 345 and cysteine 516

A redox-regulated disulphide may form within Sterol O-acyltransferase 1 between cysteines 528 and 546 (528 and 548 respectively in this structure).

Details

Redox score ?

90

PDB code

Structure name

structure of the human sterol o-acyltransferase 1 in complex with ci- 976

Structure deposition date

2019-10-16

Thiol separation (Å)

2

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

528

Residue number B

546

Peptide name

Sterol O-acyltransferase 1

Ligandability

Cysteine 528 of Sterol O-acyltransferase 1

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 546 of Sterol O-acyltransferase 1

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 Sterol O-acyltransferase 1 between cysteines 365 and 516.

Details

Redox score ?

79

PDB code

Structure name

tetrameric structure of acat1

Structure deposition date

2019-05-21

Thiol separation (Å)

3

Half-sphere exposure sum ?

73

Minimum pK_a ?

7

% buried

66

Peptide accession

Residue number A

365

Residue number B

516

Peptide name

Sterol O-acyltransferase 1

Ligandability

Cysteine 365 of Sterol O-acyltransferase 1

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 516 of Sterol O-acyltransferase 1

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 Sterol O-acyltransferase 1 between cysteines 333 and 387.

Details

Redox score ?

69

PDB code

Structure name

structure of the human sterol o-acyltransferase 1 in complex with ci- 976

Structure deposition date

2019-10-16

Thiol separation (Å)

4

Half-sphere exposure sum ?

69

Minimum pK_a ?

9

% buried

90

Peptide accession

Residue number A

333

Residue number B

387

Peptide name

Sterol O-acyltransferase 1

Ligandability

Cysteine 333 of Sterol O-acyltransferase 1

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 387 of Sterol O-acyltransferase 1

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 Sterol O-acyltransferase 1 between cysteines 345 and 365. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

46

PDB code

Structure name

structure of nevanimibe-bound human tetrameric acat1

Structure deposition date

2020-02-16

Thiol separation (Å)

9

Half-sphere exposure sum ?

66

Minimum pK_a ?

7

% buried

61

Peptide accession

Residue number A

345

Residue number B

365

Peptide name

Sterol O-acyltransferase 1

Ligandability

Cysteine 345 of Sterol O-acyltransferase 1

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 365 of Sterol O-acyltransferase 1

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 Sterol O-acyltransferase 1 between cysteines 345 and 516. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

33

PDB code

Structure name

structure of nevanimibe-bound human tetrameric acat1

Structure deposition date

2020-02-16

Thiol separation (Å)

10

Half-sphere exposure sum ?

66

Minimum pK_a ?

12

% buried

66

Peptide accession

Residue number A

345

Residue number B

516

Peptide name

Sterol O-acyltransferase 1

Ligandability

Cysteine 345 of Sterol O-acyltransferase 1

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 516 of Sterol O-acyltransferase 1

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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