ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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[F-actin]-monooxygenase MICAL1

Intramolecular
Cysteine 724 and cysteine 727
Cysteine 724 and cysteine 747
Cysteine 697 and cysteine 700
Cysteine 697 and cysteine 721
Cysteine 727 and cysteine 747
Cysteine 700 and cysteine 721
Cysteine 82 and cysteine 87
Cysteine 95 and cysteine 394
A redox-regulated disulphide may form within [F-actin]-monooxygenase MICAL1 between cysteines 724 and 727 (45 and 48 respectively in this structure).

Details

Redox score ?
93
PDB code
2co8
Structure name
solution structures of the lim domain of human nedd9 interacting protein with calponin homology and lim domains
Structure deposition date
2005-05-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
42
Minimum pKa ?
4
% buried
0
Peptide accession
Q8TDZ2
Residue number A
724
Residue number B
727
Peptide name
[F-actin]-monooxygenase MICAL1

Ligandability

Cysteine 724 of [F-actin]-monooxygenase MICAL1

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 727 of [F-actin]-monooxygenase MICAL1

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 [F-actin]-monooxygenase MICAL1 between cysteines 724 and 747 (45 and 68 respectively in this structure).

Details

Redox score ?
92
PDB code
2co8
Structure name
solution structures of the lim domain of human nedd9 interacting protein with calponin homology and lim domains
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
4
% buried
0
Peptide accession
Q8TDZ2
Residue number A
724
Residue number B
747
Peptide name
[F-actin]-monooxygenase MICAL1

Ligandability

Cysteine 724 of [F-actin]-monooxygenase MICAL1

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 747 of [F-actin]-monooxygenase MICAL1

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 [F-actin]-monooxygenase MICAL1 between cysteines 697 and 700 (18 and 21 respectively in this structure).

Details

Redox score ?
87
PDB code
2co8
Structure name
solution structures of the lim domain of human nedd9 interacting protein with calponin homology and lim domains
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
5
% buried
4
Peptide accession
Q8TDZ2
Residue number A
697
Residue number B
700
Peptide name
[F-actin]-monooxygenase MICAL1

Ligandability

Cysteine 697 of [F-actin]-monooxygenase MICAL1

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 700 of [F-actin]-monooxygenase MICAL1

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 [F-actin]-monooxygenase MICAL1 between cysteines 697 and 721 (18 and 42 respectively in this structure).

Details

Redox score ?
84
PDB code
2co8
Structure name
solution structures of the lim domain of human nedd9 interacting protein with calponin homology and lim domains
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
4
Peptide accession
Q8TDZ2
Residue number A
697
Residue number B
721
Peptide name
[F-actin]-monooxygenase MICAL1

Ligandability

Cysteine 697 of [F-actin]-monooxygenase MICAL1

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 721 of [F-actin]-monooxygenase MICAL1

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 [F-actin]-monooxygenase MICAL1 between cysteines 727 and 747 (48 and 68 respectively in this structure).

Details

Redox score ?
80
PDB code
2co8
Structure name
solution structures of the lim domain of human nedd9 interacting protein with calponin homology and lim domains
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q8TDZ2
Residue number A
727
Residue number B
747
Peptide name
[F-actin]-monooxygenase MICAL1

Ligandability

Cysteine 727 of [F-actin]-monooxygenase MICAL1

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 747 of [F-actin]-monooxygenase MICAL1

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 [F-actin]-monooxygenase MICAL1 between cysteines 700 and 721 (21 and 42 respectively in this structure).

Details

Redox score ?
77
PDB code
2co8
Structure name
solution structures of the lim domain of human nedd9 interacting protein with calponin homology and lim domains
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
9
% buried
1
Peptide accession
Q8TDZ2
Residue number A
700
Residue number B
721
Peptide name
[F-actin]-monooxygenase MICAL1

Ligandability

Cysteine 700 of [F-actin]-monooxygenase MICAL1

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 721 of [F-actin]-monooxygenase MICAL1

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 [F-actin]-monooxygenase MICAL1 between cysteines 82 and 87. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2c4c
Structure name
crystal structure of the nadph-treated monooxygenase domain of mical
Structure deposition date
2005-10-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
91
Peptide accession
Q8VDP3
Residue number A
82
Residue number B
87
Peptide name
[F-actin]-monooxygenase MICAL1

Ligandability

Cysteine 82 of [F-actin]-monooxygenase MICAL1

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 87 of [F-actin]-monooxygenase MICAL1

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 [F-actin]-monooxygenase MICAL1 between cysteines 95 and 394. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
2bry
Structure name
crystal structure of the native monooxygenase domain of mical at 1
Structure deposition date
2005-05-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
Q8VDP3
Residue number A
95
Residue number B
394
Peptide name
[F-actin]-monooxygenase MICAL1

Ligandability

Cysteine 95 of [F-actin]-monooxygenase MICAL1

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 394 of [F-actin]-monooxygenase MICAL1

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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