ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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APC variant protein

Intramolecular
Cysteine 419 and cysteine 422
Cysteine 485 and cysteine 527
Cysteine 449 and cysteine 453
Cysteine 346 and cysteine 354
Cysteine 522 and cysteine 527
A redox-regulated disulphide may form within APC variant protein between cysteines 419 and 422 (417 and 420 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3nmx
Structure name
crystal structure of apc complexed with asef
Structure deposition date
2010-06-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
65
Peptide accession
Q4LE70
Residue number A
419
Residue number B
422
Peptide name
APC variant protein

Ligandability

Cysteine 419 of APC variant protein

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 422 of APC variant protein

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 APC variant protein between cysteines 485 and 527 (483 and 525 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3nmw
Structure name
crystal structure of armadillo repeats domain of apc
Structure deposition date
2010-06-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
12
% buried
96
Peptide accession
Q4LE70
Residue number A
485
Residue number B
527
Peptide name
APC variant protein

Ligandability

Cysteine 485 of APC variant protein

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 527 of APC variant protein

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 APC variant protein between cysteines 449 and 453 (447 and 451 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3nmz
Structure name
crystal structure of apc complexed with asef
Structure deposition date
2010-06-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
51
Peptide accession
Q4LE70
Residue number A
449
Residue number B
453
Peptide name
APC variant protein

Ligandability

Cysteine 449 of APC variant protein

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 453 of APC variant protein

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 APC variant protein between cysteines 346 and 354 (344 and 352 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3nmz
Structure name
crystal structure of apc complexed with asef
Structure deposition date
2010-06-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
24
Peptide accession
Q4LE70
Residue number A
346
Residue number B
354
Peptide name
APC variant protein

Ligandability

Cysteine 346 of APC variant protein

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 354 of APC variant protein

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 APC variant protein between cysteines 522 and 527 (520 and 525 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3nmw
Structure name
crystal structure of armadillo repeats domain of apc
Structure deposition date
2010-06-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
11
% buried
87
Peptide accession
Q4LE70
Residue number A
522
Residue number B
527
Peptide name
APC variant protein

Ligandability

Cysteine 522 of APC variant protein

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 527 of APC variant protein

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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