ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

C-C motif chemokine 21

Intramolecular
Cysteine 31 and cysteine 57
Cysteine 32 and cysteine 75
Cysteine 32 and cysteine 57
Cysteine 31 and cysteine 32
Cysteine 57 and cysteine 75
Cysteine 31 and cysteine 75
A redox-regulated disulphide may form within C-C motif chemokine 21 between cysteines 31 and 57 (8 and 34 respectively in this structure).

Details

Redox score ?
86
PDB code
5eki
Structure name
crystal structure of truncated ccl21
Structure deposition date
2015-11-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00585
Residue number A
31
Residue number B
57
Peptide name
C-C motif chemokine 21

Ligandability

Cysteine 31 of C-C motif chemokine 21

Cysteine 57 of C-C motif chemokine 21

A redox-regulated disulphide may form within C-C motif chemokine 21 between cysteines 32 and 75 (9 and 52 respectively in this structure).

Details

Redox score ?
80
PDB code
5eki
Structure name
crystal structure of truncated ccl21
Structure deposition date
2015-11-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00585
Residue number A
32
Residue number B
75
Peptide name
C-C motif chemokine 21

Ligandability

Cysteine 32 of C-C motif chemokine 21

Cysteine 75 of C-C motif chemokine 21

A redox-regulated disulphide may form within C-C motif chemokine 21 between cysteines 32 and 57 (9 and 34 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
5eki
Structure name
crystal structure of truncated ccl21
Structure deposition date
2015-11-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00585
Residue number A
32
Residue number B
57
Peptide name
C-C motif chemokine 21

Ligandability

Cysteine 32 of C-C motif chemokine 21

Cysteine 57 of C-C motif chemokine 21

A redox-regulated disulphide may form within C-C motif chemokine 21 between cysteines 31 and 32 (8 and 9 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5eki
Structure name
crystal structure of truncated ccl21
Structure deposition date
2015-11-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00585
Residue number A
31
Residue number B
32
Peptide name
C-C motif chemokine 21

Ligandability

Cysteine 31 of C-C motif chemokine 21

Cysteine 32 of C-C motif chemokine 21

A redox-regulated disulphide may form within C-C motif chemokine 21 between cysteines 57 and 75 (34 and 52 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5eki
Structure name
crystal structure of truncated ccl21
Structure deposition date
2015-11-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00585
Residue number A
57
Residue number B
75
Peptide name
C-C motif chemokine 21

Ligandability

Cysteine 57 of C-C motif chemokine 21

Cysteine 75 of C-C motif chemokine 21

A redox-regulated disulphide may form within C-C motif chemokine 21 between cysteines 31 and 75 (8 and 52 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5eki
Structure name
crystal structure of truncated ccl21
Structure deposition date
2015-11-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00585
Residue number A
31
Residue number B
75
Peptide name
C-C motif chemokine 21

Ligandability

Cysteine 31 of C-C motif chemokine 21

Cysteine 75 of C-C motif chemokine 21

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