ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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N-acetyltransferase ESCO1

Intermolecular
Cysteine 757 and cysteine 757
Intramolecular
Cysteine 619 and cysteine 622
Cysteine 757 and cysteine 758
A redox-regulated disulphide may form between two units of N-acetyltransferase ESCO1 at cysteines 757 and 757.

Details

Redox score ?
79
PDB code
4mxe
Structure name
human esco1 (eco1/ctf7 ortholog), acetyltransferase domain in complex with acetyl-coa
Structure deposition date
2013-09-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide A name
N-acetyltransferase ESCO1
Peptide B name
N-acetyltransferase ESCO1
Peptide A accession
Q5FWF5
Peptide B accession
Q5FWF5
Peptide A residue number
757
Peptide B residue number
757

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.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within N-acetyltransferase ESCO1 between cysteines 619 and 622.

Details

Redox score ?
80
PDB code
5t53
Structure name
molecular basis for cohesin acetylation by establishment of sister chromatid cohesion n-acetyltransferase esco1
Structure deposition date
2016-08-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
12
Peptide accession
Q5FWF5
Residue number A
619
Residue number B
622
Peptide name
N-acetyltransferase ESCO1

Ligandability

Cysteine 619 of N-acetyltransferase ESCO1

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 622 of N-acetyltransferase ESCO1

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 N-acetyltransferase ESCO1 between cysteines 757 and 758. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4mxe
Structure name
human esco1 (eco1/ctf7 ortholog), acetyltransferase domain in complex with acetyl-coa
Structure deposition date
2013-09-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
nan
Peptide accession
Q5FWF5
Residue number A
757
Residue number B
758
Peptide name
N-acetyltransferase ESCO1

Ligandability

Cysteine 757 of N-acetyltransferase ESCO1

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 758 of N-acetyltransferase ESCO1

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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