ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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N-alpha-acetyltransferase 15, NatA auxiliary subunit

Intramolecular
Cysteine 802 and cysteine 828 L
Cysteine 465 and cysteine 484
Cysteine 20 and cysteine 33
Cysteine 465 and cysteine 491
Cysteine 448 and cysteine 465
Cysteine 484 and cysteine 491
Cysteine 491 and cysteine 508
A redox-regulated disulphide may form within N-alpha-acetyltransferase 15, NatA auxiliary subunit between cysteines 802 and 828.

Details

Redox score ?
78
PDB code
6c95
Structure name
the human nata (naa10/naa15) amino-terminal acetyltransferase complex bound to hypk
Structure deposition date
2018-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
6
% buried
57
Peptide accession
Q9BXJ9
Residue number A
802
Residue number B
828
Peptide name
N-alpha-acetyltransferase 15, NatA auxiliary subunit

Ligandability

Cysteine 802 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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.

Cysteine 828 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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-alpha-acetyltransferase 15, NatA auxiliary subunit between cysteines 465 and 484. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
6c95
Structure name
the human nata (naa10/naa15) amino-terminal acetyltransferase complex bound to hypk
Structure deposition date
2018-01-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
Q9BXJ9
Residue number A
465
Residue number B
484
Peptide name
N-alpha-acetyltransferase 15, NatA auxiliary subunit

Ligandability

Cysteine 465 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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 484 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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-alpha-acetyltransferase 15, NatA auxiliary subunit between cysteines 20 and 33. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6c95
Structure name
the human nata (naa10/naa15) amino-terminal acetyltransferase complex bound to hypk
Structure deposition date
2018-01-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
44
Peptide accession
Q9BXJ9
Residue number A
20
Residue number B
33
Peptide name
N-alpha-acetyltransferase 15, NatA auxiliary subunit

Ligandability

Cysteine 20 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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 33 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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-alpha-acetyltransferase 15, NatA auxiliary subunit between cysteines 465 and 491. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6c9m
Structure name
the human nata (naa10/naa15) amino-terminal acetyltransferase complex
Structure deposition date
2018-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
94
Peptide accession
Q9BXJ9
Residue number A
465
Residue number B
491
Peptide name
N-alpha-acetyltransferase 15, NatA auxiliary subunit

Ligandability

Cysteine 465 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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 491 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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-alpha-acetyltransferase 15, NatA auxiliary subunit between cysteines 448 and 465. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6c9m
Structure name
the human nata (naa10/naa15) amino-terminal acetyltransferase complex
Structure deposition date
2018-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
92
Peptide accession
Q9BXJ9
Residue number A
448
Residue number B
465
Peptide name
N-alpha-acetyltransferase 15, NatA auxiliary subunit

Ligandability

Cysteine 448 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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 465 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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-alpha-acetyltransferase 15, NatA auxiliary subunit between cysteines 484 and 491. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
6c9m
Structure name
the human nata (naa10/naa15) amino-terminal acetyltransferase complex
Structure deposition date
2018-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
96
Peptide accession
Q9BXJ9
Residue number A
484
Residue number B
491
Peptide name
N-alpha-acetyltransferase 15, NatA auxiliary subunit

Ligandability

Cysteine 484 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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 491 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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-alpha-acetyltransferase 15, NatA auxiliary subunit between cysteines 491 and 508. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
6pw9
Structure name
cryo-em structure of human nate/hypk complex
Structure deposition date
2019-07-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
95
Peptide accession
Q9BXJ9
Residue number A
491
Residue number B
508
Peptide name
N-alpha-acetyltransferase 15, NatA auxiliary subunit

Ligandability

Cysteine 491 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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 508 of N-alpha-acetyltransferase 15, NatA auxiliary subunit

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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