a tool for identifying drug-targetable redox-active disulphides

Abasic site processing protein HMCES

Intermolecular

Cysteine 39 and cysteine 39 L

Intramolecular

Cysteine 7 and cysteine 18

Cysteine 7 and cysteine 39 L

Cysteine 97 and cysteine 118

A redox-regulated disulphide may form between two units of Abasic site processing protein HMCES at cysteines 39 and 39.

Details

Redox score ?

80

PDB code

Structure name

crystal structure of hmces srap domain in complex with palindromic 3' overhang dna

Structure deposition date

2019-04-23

Thiol separation (Å)

2

Half-sphere exposure sum ?

68

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Abasic site processing protein HMCES

Peptide B name

Abasic site processing protein HMCES

Peptide A accession

Peptide B accession

Peptide A residue number

39

Peptide B residue number

39

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Abasic site processing protein HMCES between cysteines 7 and 18. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

42

PDB code

Structure name

crystal structure of the srap domain of human hmces protein

Structure deposition date

2016-06-29

Thiol separation (Å)

9

Half-sphere exposure sum ?

80

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

7

Residue number B

18

Peptide name

Abasic site processing protein HMCES

Ligandability

Cysteine 7 of Abasic site processing protein HMCES

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 18 of Abasic site processing protein HMCES

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 Abasic site processing protein HMCES between cysteines 7 and 39. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

35

PDB code

Structure name

crystal structure of hmces cross-linked to dna abasic site

Structure deposition date

2019-03-27

Thiol separation (Å)

10

Half-sphere exposure sum ?

68

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

7

Residue number B

39

Peptide name

Abasic site processing protein HMCES

Ligandability

Cysteine 7 of Abasic site processing protein HMCES

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 39 of Abasic site processing protein HMCES

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Abasic site processing protein HMCES between cysteines 97 and 118. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

34

PDB code

Structure name

crystal structure of the srap domain of human hmces protein

Structure deposition date

2016-06-29

Thiol separation (Å)

10

Half-sphere exposure sum ?

86

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

97

Residue number B

118

Peptide name

Abasic site processing protein HMCES

Ligandability

Cysteine 97 of Abasic site processing protein HMCES

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 118 of Abasic site processing protein HMCES

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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