ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Desmocollin-2

Intramolecular
Cysteine 669 and cysteine 677
Cysteine 585 and cysteine 671
Cysteine 471 and cysteine 559
Cysteine 669 and cysteine 671
Cysteine 671 and cysteine 677
Cysteine 585 and cysteine 669
Cysteine 585 and cysteine 677
A redox-regulated disulphide may form within Desmocollin-2 between cysteines 669 and 677 (534 and 542 respectively in this structure).

Details

Redox score ?
87
PDB code
5erp
Structure name
crystal structure of human desmocollin-2 ectodomain fragment ec2-5
Structure deposition date
2015-11-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02487
Residue number A
669
Residue number B
677
Peptide name
Desmocollin-2

Ligandability

Cysteine 669 of Desmocollin-2

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 677 of Desmocollin-2

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 Desmocollin-2 between cysteines 585 and 671 (450 and 536 respectively in this structure).

Details

Redox score ?
85
PDB code
5erp
Structure name
crystal structure of human desmocollin-2 ectodomain fragment ec2-5
Structure deposition date
2015-11-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02487
Residue number A
585
Residue number B
671
Peptide name
Desmocollin-2

Ligandability

Cysteine 585 of Desmocollin-2

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 671 of Desmocollin-2

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 Desmocollin-2 between cysteines 471 and 559 (336 and 424 respectively in this structure).

Details

Redox score ?
85
PDB code
5erp
Structure name
crystal structure of human desmocollin-2 ectodomain fragment ec2-5
Structure deposition date
2015-11-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02487
Residue number A
471
Residue number B
559
Peptide name
Desmocollin-2

Ligandability

Cysteine 471 of Desmocollin-2

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 559 of Desmocollin-2

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 Desmocollin-2 between cysteines 669 and 671 (534 and 536 respectively in this structure).

Details

Redox score ?
74
PDB code
5erp
Structure name
crystal structure of human desmocollin-2 ectodomain fragment ec2-5
Structure deposition date
2015-11-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02487
Residue number A
669
Residue number B
671
Peptide name
Desmocollin-2

Ligandability

Cysteine 669 of Desmocollin-2

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 671 of Desmocollin-2

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 Desmocollin-2 between cysteines 671 and 677 (536 and 542 respectively in this structure).

Details

Redox score ?
72
PDB code
5erp
Structure name
crystal structure of human desmocollin-2 ectodomain fragment ec2-5
Structure deposition date
2015-11-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02487
Residue number A
671
Residue number B
677
Peptide name
Desmocollin-2

Ligandability

Cysteine 671 of Desmocollin-2

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 677 of Desmocollin-2

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 Desmocollin-2 between cysteines 585 and 669 (450 and 534 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
5erp
Structure name
crystal structure of human desmocollin-2 ectodomain fragment ec2-5
Structure deposition date
2015-11-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02487
Residue number A
585
Residue number B
669
Peptide name
Desmocollin-2

Ligandability

Cysteine 585 of Desmocollin-2

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 669 of Desmocollin-2

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 Desmocollin-2 between cysteines 585 and 677 (450 and 542 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
5erp
Structure name
crystal structure of human desmocollin-2 ectodomain fragment ec2-5
Structure deposition date
2015-11-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q02487
Residue number A
585
Residue number B
677
Peptide name
Desmocollin-2

Ligandability

Cysteine 585 of Desmocollin-2

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 677 of Desmocollin-2

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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