ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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CCR4-NOT transcription complex subunit 6-like

Intramolecular
Cysteine 193 and cysteine 408
Cysteine 210 and cysteine 520
Cysteine 193 and cysteine 283
A redox-regulated disulphide may form within CCR4-NOT transcription complex subunit 6-like between cysteines 193 and 408.

Details

Redox score ?
62
PDB code
3ngn
Structure name
crystal structure of the human cnot6l nuclease domain in complex with amp
Structure deposition date
2010-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
98
Minimum pKa ?
8
% buried
100
Peptide accession
Q96LI5
Residue number A
193
Residue number B
408
Peptide name
CCR4-NOT transcription complex subunit 6-like

Ligandability

Cysteine 193 of CCR4-NOT transcription complex subunit 6-like

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 408 of CCR4-NOT transcription complex subunit 6-like

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 CCR4-NOT transcription complex subunit 6-like between cysteines 210 and 520. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3ngn
Structure name
crystal structure of the human cnot6l nuclease domain in complex with amp
Structure deposition date
2010-06-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
73
Peptide accession
Q96LI5
Residue number A
210
Residue number B
520
Peptide name
CCR4-NOT transcription complex subunit 6-like

Ligandability

Cysteine 210 of CCR4-NOT transcription complex subunit 6-like

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 520 of CCR4-NOT transcription complex subunit 6-like

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 CCR4-NOT transcription complex subunit 6-like between cysteines 193 and 283. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
5dv2
Structure name
crystal structure of human cnot6l in complex with cytidine-5'- monophosphate
Structure deposition date
2015-09-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
12
% buried
100
Peptide accession
Q96LI5
Residue number A
193
Residue number B
283
Peptide name
CCR4-NOT transcription complex subunit 6-like

Ligandability

Cysteine 193 of CCR4-NOT transcription complex subunit 6-like

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 283 of CCR4-NOT transcription complex subunit 6-like

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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