Protein spire homolog 1
Intramolecular
Cysteine 62 and cysteine 203
Cysteine 62 and cysteine 66
Cysteine 65 and cysteine 66
Cysteine 62 and cysteine 65
Cysteine 66 and cysteine 203
Cysteine 65 and cysteine 221
Cysteine 65 and cysteine 203
3rbw B 62 B 203
A redox-regulated disulphide may form within Protein spire homolog 1 between cysteines 62 and 203.
Details
Redox score ?
62
PDB code
3rbw
Structure name
crystal structure of spire kind domain
Structure deposition date
2011-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
9
% buried
100
Peptide accession
Q08AE8
Residue number A
62
Residue number B
203
Peptide name
Protein spire homolog 1
Ligandability
Cysteine 62 of Protein spire homolog 1
Cysteine 203 of Protein spire homolog 1
3r7g A 62 A 66
A redox-regulated disulphide may form within Protein spire homolog 1 between cysteines 62 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
3r7g
Structure name
crystal structure of spire kind domain in complex with the tail of fmn2
Structure deposition date
2011-03-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
99
Peptide accession
Q08AE8
Residue number A
62
Residue number B
66
Peptide name
Protein spire homolog 1
Ligandability
Cysteine 62 of Protein spire homolog 1
Cysteine 66 of Protein spire homolog 1
3rbw B 65 B 66
A redox-regulated disulphide may form within Protein spire homolog 1 between cysteines 65 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3rbw
Structure name
crystal structure of spire kind domain
Structure deposition date
2011-03-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
85
Minimum pKa ?
13
% buried
100
Peptide accession
Q08AE8
Residue number A
65
Residue number B
66
Peptide name
Protein spire homolog 1
Ligandability
Cysteine 65 of Protein spire homolog 1
Cysteine 66 of Protein spire homolog 1
3rbw A 62 A 65
A redox-regulated disulphide may form within Protein spire homolog 1 between cysteines 62 and 65. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3rbw
Structure name
crystal structure of spire kind domain
Structure deposition date
2011-03-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
95
Minimum pKa ?
9
% buried
100
Peptide accession
Q08AE8
Residue number A
62
Residue number B
65
Peptide name
Protein spire homolog 1
Ligandability
Cysteine 62 of Protein spire homolog 1
Cysteine 65 of Protein spire homolog 1
3rbw A 66 A 203
A redox-regulated disulphide may form within Protein spire homolog 1 between cysteines 66 and 203. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3rbw
Structure name
crystal structure of spire kind domain
Structure deposition date
2011-03-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
14
% buried
100
Peptide accession
Q08AE8
Residue number A
66
Residue number B
203
Peptide name
Protein spire homolog 1
Ligandability
Cysteine 66 of Protein spire homolog 1
Cysteine 203 of Protein spire homolog 1
3rbw D 65 D 221
A redox-regulated disulphide may form within Protein spire homolog 1 between cysteines 65 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
3rbw
Structure name
crystal structure of spire kind domain
Structure deposition date
2011-03-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
95
Peptide accession
Q08AE8
Residue number A
65
Residue number B
221
Peptide name
Protein spire homolog 1
Ligandability
Cysteine 65 of Protein spire homolog 1
Cysteine 221 of Protein spire homolog 1
3rbw B 65 B 203
A redox-regulated disulphide may form within Protein spire homolog 1 between cysteines 65 and 203. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
3rbw
Structure name
crystal structure of spire kind domain
Structure deposition date
2011-03-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
100
Peptide accession
Q08AE8
Residue number A
65
Residue number B
203
Peptide name
Protein spire homolog 1
Ligandability
Cysteine 65 of Protein spire homolog 1
Cysteine 203 of Protein spire homolog 1
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