ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Adenomatous polyposis coli protein

Intermolecular
Cysteine 121 of Axin-1 and cysteine 2042
Intramolecular
Cysteine 447 and cysteine 451
Cysteine 417 and cysteine 420
Cysteine 483 and cysteine 525
Cysteine 520 and cysteine 525
A redox-regulated disulphide may form between cysteine 121 of Axin-1 and cysteine 2042 of Adenomatous polyposis coli protein (158 and 2043 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
1emu
Structure name
structure of the axin rgs-homologous domain in complex with a samp repeat from apc
Structure deposition date
2000-03-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
86
Peptide A name
Axin-1
Peptide B name
Adenomatous polyposis coli protein
Peptide A accession
O15169
Peptide B accession
P25054
Peptide A residue number
121
Peptide B residue number
2042

Ligandability

Cysteine 121 of Axin-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 2042 of Adenomatous polyposis coli 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 Adenomatous polyposis coli protein between cysteines 447 and 451. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3au3
Structure name
crystal structure of armadillo repeat domain of apc
Structure deposition date
2011-01-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
27
Peptide accession
P25054
Residue number A
447
Residue number B
451
Peptide name
Adenomatous polyposis coli protein

Ligandability

Cysteine 447 of Adenomatous polyposis coli 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 451 of Adenomatous polyposis coli 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 Adenomatous polyposis coli protein between cysteines 417 and 420. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3t7u
Structure name
a new crystal structure of apc-arm
Structure deposition date
2011-07-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
54
Peptide accession
P25054
Residue number A
417
Residue number B
420
Peptide name
Adenomatous polyposis coli protein

Ligandability

Cysteine 417 of Adenomatous polyposis coli 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 420 of Adenomatous polyposis coli 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 Adenomatous polyposis coli protein between cysteines 483 and 525. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3t7u
Structure name
a new crystal structure of apc-arm
Structure deposition date
2011-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
84
Peptide accession
P25054
Residue number A
483
Residue number B
525
Peptide name
Adenomatous polyposis coli protein

Ligandability

Cysteine 483 of Adenomatous polyposis coli 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 525 of Adenomatous polyposis coli 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 Adenomatous polyposis coli protein between cysteines 520 and 525. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3qhe
Structure name
crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of sam68
Structure deposition date
2011-01-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
88
Peptide accession
P25054
Residue number A
520
Residue number B
525
Peptide name
Adenomatous polyposis coli protein

Ligandability

Cysteine 520 of Adenomatous polyposis coli 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 525 of Adenomatous polyposis coli 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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