ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Autophagy-related protein 16-1

Intramolecular
Cysteine 506 and cysteine 533
Cysteine 316 and cysteine 356
Cysteine 457 and cysteine 461
A redox-regulated disulphide may form within Autophagy-related protein 16-1 between cysteines 506 and 533.

Details

Redox score ?
70
PDB code
5nuv
Structure name
structure of the wd40-domain of human atg16l1
Structure deposition date
2017-05-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
90
Minimum pKa ?
8
% buried
89
Peptide accession
Q676U5
Residue number A
506
Residue number B
533
Peptide name
Autophagy-related protein 16-1

Ligandability

Cysteine 506 of Autophagy-related protein 16-1

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 533 of Autophagy-related protein 16-1

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.

A redox-regulated disulphide may form within Autophagy-related protein 16-1 between cysteines 316 and 356.

Details

Redox score ?
66
PDB code
5nuv
Structure name
structure of the wd40-domain of human atg16l1
Structure deposition date
2017-05-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
51
Peptide accession
Q676U5
Residue number A
316
Residue number B
356
Peptide name
Autophagy-related protein 16-1

Ligandability

Cysteine 316 of Autophagy-related protein 16-1

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 356 of Autophagy-related protein 16-1

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.

A redox-regulated disulphide may form within Autophagy-related protein 16-1 between cysteines 457 and 461. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
5nuv
Structure name
structure of the wd40-domain of human atg16l1
Structure deposition date
2017-05-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
76
Peptide accession
Q676U5
Residue number A
457
Residue number B
461
Peptide name
Autophagy-related protein 16-1

Ligandability

Cysteine 457 of Autophagy-related protein 16-1

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 461 of Autophagy-related protein 16-1

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.

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