ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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C-type lectin domain family 4 member M

Intermolecular
Cysteine 265 and cysteine 395
Intramolecular
Cysteine 268 and cysteine 279
Cysteine 296 and cysteine 389
Cysteine 368 and cysteine 381
A redox-regulated disulphide may form between two units of C-type lectin domain family 4 member M at cysteines 265 and 395. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1xar
Structure name
crystal structure of a fragment of dc-signr (containing the carbohydrate recognition domain and two repeats of the neck)
Structure deposition date
2004-08-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide A name
C-type lectin domain family 4 member M
Peptide B name
C-type lectin domain family 4 member M
Peptide A accession
Q9H2X3
Peptide B accession
Q9H2X3
Peptide A residue number
265
Peptide B residue number
395

Ligandability

Cysteine 265 of C-type lectin domain family 4 member M

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 395 of C-type lectin domain family 4 member M

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 C-type lectin domain family 4 member M between cysteines 268 and 279.

Details

Redox score ?
85
PDB code
1xar
Structure name
crystal structure of a fragment of dc-signr (containing the carbohydrate recognition domain and two repeats of the neck)
Structure deposition date
2004-08-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2X3
Residue number A
268
Residue number B
279
Peptide name
C-type lectin domain family 4 member M

Ligandability

Cysteine 268 of C-type lectin domain family 4 member M

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 279 of C-type lectin domain family 4 member M

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 C-type lectin domain family 4 member M between cysteines 296 and 389.

Details

Redox score ?
83
PDB code
1xar
Structure name
crystal structure of a fragment of dc-signr (containing the carbohydrate recognition domain and two repeats of the neck)
Structure deposition date
2004-08-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2X3
Residue number A
296
Residue number B
389
Peptide name
C-type lectin domain family 4 member M

Ligandability

Cysteine 296 of C-type lectin domain family 4 member M

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 389 of C-type lectin domain family 4 member M

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 C-type lectin domain family 4 member M between cysteines 368 and 381.

Details

Redox score ?
82
PDB code
1xar
Structure name
crystal structure of a fragment of dc-signr (containing the carbohydrate recognition domain and two repeats of the neck)
Structure deposition date
2004-08-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2X3
Residue number A
368
Residue number B
381
Peptide name
C-type lectin domain family 4 member M

Ligandability

Cysteine 368 of C-type lectin domain family 4 member M

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 381 of C-type lectin domain family 4 member M

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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