ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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F-actin-uncapping protein LRRC16A

Intramolecular
Cysteine 51 and cysteine 165
Cysteine 51 and cysteine 113
Cysteine 390 and cysteine 393
Cysteine 377 and cysteine 383
Cysteine 51 and cysteine 167
Cysteine 464 and cysteine 469
Cysteine 113 and cysteine 165
Cysteine 165 and cysteine 167
Cysteine 383 and cysteine 390
A redox-regulated disulphide may form within F-actin-uncapping protein LRRC16A between cysteines 51 and 165.

Details

Redox score ?
74
PDB code
4k17
Structure name
crystal structure of mouse carmil residues 1-668
Structure deposition date
2013-04-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
78
Peptide accession
Q6EDY6
Residue number A
51
Residue number B
165
Peptide name
F-actin-uncapping protein LRRC16A

Ligandability

Cysteine 51 of F-actin-uncapping protein LRRC16A

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 165 of F-actin-uncapping protein LRRC16A

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-uncapping protein LRRC16A between cysteines 51 and 113. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4k17
Structure name
crystal structure of mouse carmil residues 1-668
Structure deposition date
2013-04-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
69
Peptide accession
Q6EDY6
Residue number A
51
Residue number B
113
Peptide name
F-actin-uncapping protein LRRC16A

Ligandability

Cysteine 51 of F-actin-uncapping protein LRRC16A

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 113 of F-actin-uncapping protein LRRC16A

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-uncapping protein LRRC16A between cysteines 390 and 393. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4k17
Structure name
crystal structure of mouse carmil residues 1-668
Structure deposition date
2013-04-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
50
Peptide accession
Q6EDY6
Residue number A
390
Residue number B
393
Peptide name
F-actin-uncapping protein LRRC16A

Ligandability

Cysteine 390 of F-actin-uncapping protein LRRC16A

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 393 of F-actin-uncapping protein LRRC16A

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-uncapping protein LRRC16A between cysteines 377 and 383. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4k17
Structure name
crystal structure of mouse carmil residues 1-668
Structure deposition date
2013-04-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
98
Peptide accession
Q6EDY6
Residue number A
377
Residue number B
383
Peptide name
F-actin-uncapping protein LRRC16A

Ligandability

Cysteine 377 of F-actin-uncapping protein LRRC16A

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 383 of F-actin-uncapping protein LRRC16A

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-uncapping protein LRRC16A between cysteines 51 and 167. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4k17
Structure name
crystal structure of mouse carmil residues 1-668
Structure deposition date
2013-04-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
64
Peptide accession
Q6EDY6
Residue number A
51
Residue number B
167
Peptide name
F-actin-uncapping protein LRRC16A

Ligandability

Cysteine 51 of F-actin-uncapping protein LRRC16A

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 167 of F-actin-uncapping protein LRRC16A

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-uncapping protein LRRC16A between cysteines 464 and 469. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4k17
Structure name
crystal structure of mouse carmil residues 1-668
Structure deposition date
2013-04-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
60
Peptide accession
Q6EDY6
Residue number A
464
Residue number B
469
Peptide name
F-actin-uncapping protein LRRC16A

Ligandability

Cysteine 464 of F-actin-uncapping protein LRRC16A

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 469 of F-actin-uncapping protein LRRC16A

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-uncapping protein LRRC16A between cysteines 113 and 165. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4k17
Structure name
crystal structure of mouse carmil residues 1-668
Structure deposition date
2013-04-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
83
Peptide accession
Q6EDY6
Residue number A
113
Residue number B
165
Peptide name
F-actin-uncapping protein LRRC16A

Ligandability

Cysteine 113 of F-actin-uncapping protein LRRC16A

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 165 of F-actin-uncapping protein LRRC16A

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-uncapping protein LRRC16A between cysteines 165 and 167. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4k17
Structure name
crystal structure of mouse carmil residues 1-668
Structure deposition date
2013-04-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
12
% buried
nan
Peptide accession
Q6EDY6
Residue number A
165
Residue number B
167
Peptide name
F-actin-uncapping protein LRRC16A

Ligandability

Cysteine 165 of F-actin-uncapping protein LRRC16A

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 167 of F-actin-uncapping protein LRRC16A

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-uncapping protein LRRC16A between cysteines 383 and 390. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
4k17
Structure name
crystal structure of mouse carmil residues 1-668
Structure deposition date
2013-04-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
96
Peptide accession
Q6EDY6
Residue number A
383
Residue number B
390
Peptide name
F-actin-uncapping protein LRRC16A

Ligandability

Cysteine 383 of F-actin-uncapping protein LRRC16A

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 390 of F-actin-uncapping protein LRRC16A

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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