ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

N-chimaerin

Intramolecular
Cysteine 35 and cysteine 37
Cysteine 236 and cysteine 239
Cysteine 236 and cysteine 255
Cysteine 239 and cysteine 255
Cysteine 219 and cysteine 247
Cysteine 222 and cysteine 247
Cysteine 219 and cysteine 222
A redox-regulated disulphide may form within N-chimaerin between cysteines 35 and 37.

Details

Redox score ?
78
PDB code
3cxl
Structure name
crystal structure of human chimerin 1 (chn1)
Structure deposition date
2008-04-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15882
Residue number A
35
Residue number B
37
Peptide name
N-chimaerin

Ligandability

Cysteine 35 of N-chimaerin

Cysteine 37 of N-chimaerin

A redox-regulated disulphide may form within N-chimaerin between cysteines 236 and 239.

Details

Redox score ?
77
PDB code
3cxl
Structure name
crystal structure of human chimerin 1 (chn1)
Structure deposition date
2008-04-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15882
Residue number A
236
Residue number B
239
Peptide name
N-chimaerin

Ligandability

Cysteine 236 of N-chimaerin

Cysteine 239 of N-chimaerin

A redox-regulated disulphide may form within N-chimaerin between cysteines 236 and 255.

Details

Redox score ?
76
PDB code
3cxl
Structure name
crystal structure of human chimerin 1 (chn1)
Structure deposition date
2008-04-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15882
Residue number A
236
Residue number B
255
Peptide name
N-chimaerin

Ligandability

Cysteine 236 of N-chimaerin

Cysteine 255 of N-chimaerin

A redox-regulated disulphide may form within N-chimaerin between cysteines 239 and 255.

Details

Redox score ?
75
PDB code
3cxl
Structure name
crystal structure of human chimerin 1 (chn1)
Structure deposition date
2008-04-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15882
Residue number A
239
Residue number B
255
Peptide name
N-chimaerin

Ligandability

Cysteine 239 of N-chimaerin

Cysteine 255 of N-chimaerin

A redox-regulated disulphide may form within N-chimaerin between cysteines 219 and 247.

Details

Redox score ?
73
PDB code
3cxl
Structure name
crystal structure of human chimerin 1 (chn1)
Structure deposition date
2008-04-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15882
Residue number A
219
Residue number B
247
Peptide name
N-chimaerin

Ligandability

Cysteine 219 of N-chimaerin

Cysteine 247 of N-chimaerin

A redox-regulated disulphide may form within N-chimaerin between cysteines 222 and 247.

Details

Redox score ?
72
PDB code
3cxl
Structure name
crystal structure of human chimerin 1 (chn1)
Structure deposition date
2008-04-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15882
Residue number A
222
Residue number B
247
Peptide name
N-chimaerin

Ligandability

Cysteine 222 of N-chimaerin

Cysteine 247 of N-chimaerin

A redox-regulated disulphide may form within N-chimaerin between cysteines 219 and 222.

Details

Redox score ?
72
PDB code
3cxl
Structure name
crystal structure of human chimerin 1 (chn1)
Structure deposition date
2008-04-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15882
Residue number A
219
Residue number B
222
Peptide name
N-chimaerin

Ligandability

Cysteine 219 of N-chimaerin

Cysteine 222 of N-chimaerin

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