ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Checkpoint protein HUS1

Intermolecular
Cysteine 200 and cysteine 132 of Cell cycle checkpoint protein RAD1
Cysteine 200 and cysteine 92 of Cell cycle checkpoint protein RAD1
Intramolecular
Cysteine 30 and cysteine 44
Cysteine 30 and cysteine 56
A redox-regulated disulphide may form between cysteine 200 of Checkpoint protein HUS1 and cysteine 132 of Cell cycle checkpoint protein RAD1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6j8y
Structure name
crystal structure of the human rad9-hus1-rad1-rhino complex
Structure deposition date
2019-01-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
62
Peptide A name
Checkpoint protein HUS1
Peptide B name
Cell cycle checkpoint protein RAD1
Peptide A accession
O60921
Peptide B accession
O60671
Peptide A residue number
200
Peptide B residue number
132

Ligandability

Cysteine 200 of Checkpoint protein HUS1

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 132 of Cell cycle checkpoint protein RAD1

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 cysteine 200 of Checkpoint protein HUS1 and cysteine 92 of Cell cycle checkpoint protein RAD1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
6j8y
Structure name
crystal structure of the human rad9-hus1-rad1-rhino complex
Structure deposition date
2019-01-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
62
Peptide A name
Checkpoint protein HUS1
Peptide B name
Cell cycle checkpoint protein RAD1
Peptide A accession
O60921
Peptide B accession
O60671
Peptide A residue number
200
Peptide B residue number
92

Ligandability

Cysteine 200 of Checkpoint protein HUS1

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 92 of Cell cycle checkpoint protein RAD1

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 Checkpoint protein HUS1 between cysteines 30 and 44. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6j8y
Structure name
crystal structure of the human rad9-hus1-rad1-rhino complex
Structure deposition date
2019-01-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
70
Peptide accession
O60921
Residue number A
30
Residue number B
44
Peptide name
Checkpoint protein HUS1

Ligandability

Cysteine 30 of Checkpoint protein HUS1

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 44 of Checkpoint protein HUS1

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 Checkpoint protein HUS1 between cysteines 30 and 56. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3g65
Structure name
crystal structure of the human rad9-rad1-hus1 dna damage checkpoint complex
Structure deposition date
2009-02-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
93
Peptide accession
O60921
Residue number A
30
Residue number B
56
Peptide name
Checkpoint protein HUS1

Ligandability

Cysteine 30 of Checkpoint protein HUS1

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 56 of Checkpoint protein HUS1

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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