ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Myosin-7

Intermolecular
Cysteine 905 and cysteine 905
Cysteine 947 and cysteine 947
Cysteine 1748 and cysteine 1748
Intramolecular
Cysteine 175 and cysteine 672
Cysteine 122 and cysteine 672
Cysteine 122 and cysteine 705
Cysteine 122 and cysteine 175
Cysteine 1249 and cysteine 130
A redox-regulated disulphide may form between two units of Myosin-7 at cysteines 905 and 905.

Details

Redox score ?
83
PDB code
2fxo
Structure name
structure of the human beta-myosin s2 fragment
Structure deposition date
2006-02-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
9
Peptide A name
Myosin-7
Peptide B name
Myosin-7
Peptide A accession
P12883
Peptide B accession
P12883
Peptide A residue number
905
Peptide B residue number
905

Ligandability

A redox-regulated disulphide may form between two units of Myosin-7 at cysteines 947 and 947.

Details

Redox score ?
75
PDB code
2fxm
Structure name
structure of the human beta-myosin s2 fragment
Structure deposition date
2006-02-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
3
Peptide A name
Myosin-7
Peptide B name
Myosin-7
Peptide A accession
P12883
Peptide B accession
P12883
Peptide A residue number
947
Peptide B residue number
947

Ligandability

A redox-regulated disulphide may form between two units of Myosin-7 at cysteines 1748 and 1748.

Details

Redox score ?
67
PDB code
5wjb
Structure name
crystal structure of amino acids 1733-1797 of human beta cardiac myosin fused to gp7
Structure deposition date
2017-07-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
0
Peptide A name
Myosin-7
Peptide B name
Myosin-7
Peptide A accession
P12883
Peptide B accession
P12883
Peptide A residue number
1748
Peptide B residue number
1748

Ligandability

A redox-regulated disulphide may form within Myosin-7 between cysteines 175 and 672 (175 and 684 respectively in this structure).

Details

Redox score ?
65
PDB code
3dtp
Structure name
tarantula heavy meromyosin obtained by flexible docking to tarantula muscle thick filament cryo-em 3d-map
Structure deposition date
2008-07-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
103
Minimum pKa ?
8
% buried
100
Peptide accession
P12883
Residue number A
175
Residue number B
672
Peptide name
Myosin-7

Ligandability

Cysteine 175 of Myosin-7

Cysteine 672 of Myosin-7

Cysteine 175 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Myosin-7 between cysteines 122 and 672. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4db1
Structure name
cardiac human myosin s1dc, beta isoform complexed with mn-amppnp
Structure deposition date
2012-01-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
P12883
Residue number A
122
Residue number B
672
Peptide name
Myosin-7

Ligandability

Cysteine 122 of Myosin-7

Cysteine 672 of Myosin-7

A redox-regulated disulphide may form within Myosin-7 between cysteines 122 and 705. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
5tby
Structure name
human beta cardiac heavy meromyosin interacting-heads motif obtained by homology modeling (using swiss-model) of human sequence from aphonopelma homology model (pdb-3jbh), rigidly fitted to human beta- cardiac negatively stained thick filament 3d-reconstruction (emd- 2240)
Structure deposition date
2016-09-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
P12883
Residue number A
122
Residue number B
705
Peptide name
Myosin-7

Ligandability

Cysteine 122 of Myosin-7

Cysteine 705 of Myosin-7

A redox-regulated disulphide may form within Myosin-7 between cysteines 122 and 175 (121 and 175 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
3dtp
Structure name
tarantula heavy meromyosin obtained by flexible docking to tarantula muscle thick filament cryo-em 3d-map
Structure deposition date
2008-07-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
103
Minimum pKa ?
13
% buried
100
Peptide accession
P12883
Residue number A
122
Residue number B
175
Peptide name
Myosin-7

Ligandability

Cysteine 122 of Myosin-7

Cysteine 175 of Myosin-7

Cysteine 175 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Myosin-7 between cysteines 1249 and 130 (128 and 130 respectively in this structure).

Details

Redox score ?
nan
PDB code
5cj0
Structure name
crystal structure of amino acids 1631-1692 of myh7
Structure deposition date
2015-07-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
66
Peptide accession
P12883
Residue number A
1249
Residue number B
130
Peptide name
Myosin-7

Ligandability

Cysteine 1249 of Myosin-7

Cysteine 130 of Myosin-7

Uncertain whether structure cysteine 128 has been assigned to correct residue.
Cysteine 130 in protein B could not be asigned to a Uniprot residue.
If this tool was useful for finding a disulphide, please cite: