ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Nuclear mitotic apparatus protein 1

Intermolecular
Cysteine 161 of G-protein-signaling modulator 2 and cysteine 1907
Intramolecular
Cysteine 65 and cysteine 80 L
Cysteine 33 and cysteine 65 L
A redox-regulated disulphide may form between cysteine 161 of G-protein-signaling modulator 2 and cysteine 1907 of Nuclear mitotic apparatus protein 1 (154 and 1907 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6hc2
Structure name
crystal structure of numa/lgn hetero-hexamers
Structure deposition date
2018-08-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
56
Peptide A name
G-protein-signaling modulator 2
Peptide B name
Nuclear mitotic apparatus protein 1
Peptide A accession
P81274
Peptide B accession
Q14980
Peptide A residue number
161
Peptide B residue number
1907

Ligandability

Cysteine 161 of G-protein-signaling modulator 2

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 1907 of Nuclear mitotic apparatus protein 1

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 Nuclear mitotic apparatus protein 1 between cysteines 65 and 80. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
6qja
Structure name
organizational principles of the numa-dynein interaction interface and implications for mitotic spindle functions
Structure deposition date
2019-01-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
42
Peptide accession
Q14980
Residue number A
65
Residue number B
80
Peptide name
Nuclear mitotic apparatus protein 1

Ligandability

Cysteine 65 of Nuclear mitotic apparatus protein 1

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.

Ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 80 of Nuclear mitotic apparatus protein 1

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.

A redox-regulated disulphide may form within Nuclear mitotic apparatus protein 1 between cysteines 33 and 65. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6qja
Structure name
organizational principles of the numa-dynein interaction interface and implications for mitotic spindle functions
Structure deposition date
2019-01-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
65
Peptide accession
Q14980
Residue number A
33
Residue number B
65
Peptide name
Nuclear mitotic apparatus protein 1

Ligandability

Cysteine 33 of Nuclear mitotic apparatus protein 1

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 65 of Nuclear mitotic apparatus protein 1

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.

Ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

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