ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Centromere protein L

Intermolecular
Cysteine 286 and cysteine 293 of Centromere protein N
Intramolecular
Cysteine 52 and cysteine 228 L
Cysteine 52 and cysteine 324 L
Cysteine 228 and cysteine 324
Cysteine 164 and cysteine 180
Cysteine 163 and cysteine 164
A redox-regulated disulphide may form between cysteine 286 of Centromere protein L and cysteine 293 of Centromere protein N. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7yyh
Structure name
structure of the human ccandeltat cenp-a alpha-satellite complex
Structure deposition date
2022-02-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
74
Peptide A name
Centromere protein L
Peptide B name
Centromere protein N
Peptide A accession
Q8N0S6
Peptide B accession
Q96H22
Peptide A residue number
286
Peptide B residue number
293

Ligandability

Cysteine 286 of Centromere protein L

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 293 of Centromere protein N

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 Centromere protein L between cysteines 52 and 228. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
7xho
Structure name
structure of human inner kinetochore ccan complex
Structure deposition date
2022-04-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
52
Peptide accession
Q8N0S6
Residue number A
52
Residue number B
228
Peptide name
Centromere protein L

Ligandability

Cysteine 52 of Centromere protein L

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.

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 228 of Centromere protein L

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 Centromere protein L between cysteines 52 and 324. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7pkn
Structure name
structure of the human ccan deltact complex
Structure deposition date
2021-08-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
14
Peptide accession
Q8N0S6
Residue number A
52
Residue number B
324
Peptide name
Centromere protein L

Ligandability

Cysteine 52 of Centromere protein L

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.

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 324 of Centromere protein L

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 Centromere protein L between cysteines 228 and 324. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
7r5s
Structure name
structure of the human ccan bound to alpha satellite dna
Structure deposition date
2022-02-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
53
Peptide accession
Q8N0S6
Residue number A
228
Residue number B
324
Peptide name
Centromere protein L

Ligandability

Cysteine 228 of Centromere protein L

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 324 of Centromere protein L

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 Centromere protein L between cysteines 164 and 180. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
7r5s
Structure name
structure of the human ccan bound to alpha satellite dna
Structure deposition date
2022-02-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
86
Peptide accession
Q8N0S6
Residue number A
164
Residue number B
180
Peptide name
Centromere protein L

Ligandability

Cysteine 164 of Centromere protein L

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 180 of Centromere protein L

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 Centromere protein L between cysteines 163 and 164. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7xhn
Structure name
structure of human inner kinetochore ccan-dna complex
Structure deposition date
2022-04-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
13
% buried
100
Peptide accession
Q8N0S6
Residue number A
163
Residue number B
164
Peptide name
Centromere protein L

Ligandability

Cysteine 163 of Centromere protein L

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 164 of Centromere protein L

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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