Hsp70-binding protein 1
Intramolecular
Cysteine 310 and cysteine 348
Cysteine 325 and cysteine 341
Cysteine 131 and cysteine 172
Cysteine 141 and cysteine 172
Cysteine 131 and cysteine 141
Cysteine 269 and cysteine 310
Cysteine 297 and cysteine 348
Cysteine 96 and cysteine 131
Cysteine 297 and cysteine 310
Cysteine 172 and cysteine 214
Cysteine 297 and cysteine 341
1xqr B 310 B 348
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 310 and 348.
Details
Redox score ?
77
PDB code
1xqr
Structure name
crystal structure of the hspbp1 core domain
Structure deposition date
2004-10-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
64
Peptide accession
Q9NZL4
Residue number A
310
Residue number B
348
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 310 of Hsp70-binding protein 1
Cysteine 348 of Hsp70-binding protein 1
1xqs B 325 B 341
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 325 and 341.
Details
Redox score ?
77
PDB code
1xqs
Structure name
crystal structure of the hspbp1 core domain complexed with the fragment of hsp70 atpase domain
Structure deposition date
2004-10-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
34
Peptide accession
Q9NZL4
Residue number A
325
Residue number B
341
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 325 of Hsp70-binding protein 1
Cysteine 341 of Hsp70-binding protein 1
1xqs A 131 A 172
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 131 and 172.
Details
Redox score ?
70
PDB code
1xqs
Structure name
crystal structure of the hspbp1 core domain complexed with the fragment of hsp70 atpase domain
Structure deposition date
2004-10-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
9
% buried
100
Peptide accession
Q9NZL4
Residue number A
131
Residue number B
172
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 131 of Hsp70-binding protein 1
Cysteine 172 of Hsp70-binding protein 1
1xqr B 141 B 172
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 141 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
1xqr
Structure name
crystal structure of the hspbp1 core domain
Structure deposition date
2004-10-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
78
Peptide accession
Q9NZL4
Residue number A
141
Residue number B
172
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 141 of Hsp70-binding protein 1
Cysteine 172 of Hsp70-binding protein 1
1xqr A 131 A 141
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 131 and 141. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
1xqr
Structure name
crystal structure of the hspbp1 core domain
Structure deposition date
2004-10-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
72
Peptide accession
Q9NZL4
Residue number A
131
Residue number B
141
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 131 of Hsp70-binding protein 1
Cysteine 141 of Hsp70-binding protein 1
1xqr A 269 A 310
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 269 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
1xqr
Structure name
crystal structure of the hspbp1 core domain
Structure deposition date
2004-10-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
62
Peptide accession
Q9NZL4
Residue number A
269
Residue number B
310
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 269 of Hsp70-binding protein 1
Cysteine 310 of Hsp70-binding protein 1
1xqs A 297 A 348
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 297 and 348. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
1xqs
Structure name
crystal structure of the hspbp1 core domain complexed with the fragment of hsp70 atpase domain
Structure deposition date
2004-10-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
54
Peptide accession
Q9NZL4
Residue number A
297
Residue number B
348
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 297 of Hsp70-binding protein 1
Cysteine 348 of Hsp70-binding protein 1
1xqs A 96 A 131
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 96 and 131. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
1xqs
Structure name
crystal structure of the hspbp1 core domain complexed with the fragment of hsp70 atpase domain
Structure deposition date
2004-10-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
74
Peptide accession
Q9NZL4
Residue number A
96
Residue number B
131
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 96 of Hsp70-binding protein 1
Cysteine 131 of Hsp70-binding protein 1
1xqr A 297 A 310
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 297 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
1xqr
Structure name
crystal structure of the hspbp1 core domain
Structure deposition date
2004-10-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
79
Peptide accession
Q9NZL4
Residue number A
297
Residue number B
310
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 297 of Hsp70-binding protein 1
Cysteine 310 of Hsp70-binding protein 1
1xqs B 172 B 214
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 172 and 214. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
1xqs
Structure name
crystal structure of the hspbp1 core domain complexed with the fragment of hsp70 atpase domain
Structure deposition date
2004-10-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
100
Peptide accession
Q9NZL4
Residue number A
172
Residue number B
214
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 172 of Hsp70-binding protein 1
Cysteine 214 of Hsp70-binding protein 1
1xqs A 297 A 341
A redox-regulated disulphide may form within Hsp70-binding protein 1 between cysteines 297 and 341. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
1xqs
Structure name
crystal structure of the hspbp1 core domain complexed with the fragment of hsp70 atpase domain
Structure deposition date
2004-10-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
68
Peptide accession
Q9NZL4
Residue number A
297
Residue number B
341
Peptide name
Hsp70-binding protein 1
Ligandability
Cysteine 297 of Hsp70-binding protein 1
Cysteine 341 of Hsp70-binding protein 1
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