C-C motif chemokine 26
Intramolecular
Cysteine 33 and cysteine 57
Cysteine 34 and cysteine 73
Cysteine 34 and cysteine 57
Cysteine 33 and cysteine 34
Cysteine 57 and cysteine 73
Cysteine 33 and cysteine 73
1g2s A 10 A 34
A redox-regulated disulphide may form within C-C motif chemokine 26 between cysteines 33 and 57 (10 and 34 respectively in this structure).
Details
Redox score ?
88
PDB code
1g2s
Structure name
solution structure of eotaxin-3
Structure deposition date
2000-10-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y258
Residue number A
33
Residue number B
57
Peptide name
C-C motif chemokine 26
Ligandability
Cysteine 33 of C-C motif chemokine 26
Cysteine 57 of C-C motif chemokine 26
1g2t A 11 A 50
A redox-regulated disulphide may form within C-C motif chemokine 26 between cysteines 34 and 73 (11 and 50 respectively in this structure).
Details
Redox score ?
85
PDB code
1g2t
Structure name
solution structure of eotaxin-3
Structure deposition date
2000-10-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y258
Residue number A
34
Residue number B
73
Peptide name
C-C motif chemokine 26
Ligandability
Cysteine 34 of C-C motif chemokine 26
Cysteine 73 of C-C motif chemokine 26
1g2s A 11 A 34
A redox-regulated disulphide may form within C-C motif chemokine 26 between cysteines 34 and 57 (11 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 ?
59
PDB code
1g2s
Structure name
solution structure of eotaxin-3
Structure deposition date
2000-10-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y258
Residue number A
34
Residue number B
57
Peptide name
C-C motif chemokine 26
Ligandability
Cysteine 34 of C-C motif chemokine 26
Cysteine 57 of C-C motif chemokine 26
1g2s A 10 A 11
A redox-regulated disulphide may form within C-C motif chemokine 26 between cysteines 33 and 34 (10 and 11 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
1g2s
Structure name
solution structure of eotaxin-3
Structure deposition date
2000-10-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y258
Residue number A
33
Residue number B
34
Peptide name
C-C motif chemokine 26
Ligandability
Cysteine 33 of C-C motif chemokine 26
Cysteine 34 of C-C motif chemokine 26
1g2s A 34 A 50
A redox-regulated disulphide may form within C-C motif chemokine 26 between cysteines 57 and 73 (34 and 50 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
1g2s
Structure name
solution structure of eotaxin-3
Structure deposition date
2000-10-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y258
Residue number A
57
Residue number B
73
Peptide name
C-C motif chemokine 26
Ligandability
Cysteine 57 of C-C motif chemokine 26
Cysteine 73 of C-C motif chemokine 26
1g2s A 10 A 50
A redox-regulated disulphide may form within C-C motif chemokine 26 between cysteines 33 and 73 (10 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
1g2s
Structure name
solution structure of eotaxin-3
Structure deposition date
2000-10-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y258
Residue number A
33
Residue number B
73
Peptide name
C-C motif chemokine 26
Ligandability
Cysteine 33 of C-C motif chemokine 26
Cysteine 73 of C-C motif chemokine 26
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