Heat shock protein 105 kDa
Intramolecular
Cysteine 140 and cysteine 167
Cysteine 167 and cysteine 380
Cysteine 167 and cysteine 376 L
Cysteine 140 and cysteine 380
Cysteine 376 and cysteine 380 L
Cysteine 245 and cysteine 270
Cysteine 13 and cysteine 34
Cysteine 140 and cysteine 376 L
6gfa A 139 A 166
A redox-regulated disulphide may form within Heat shock protein 105 kDa between cysteines 140 and 167 (139 and 166 respectively in this structure).
Details
Redox score ?
74
PDB code
6gfa
Structure name
structure of nucleotide binding domain of hsp110, atp and mg2+ complexed
Structure deposition date
2018-04-29
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
69
Peptide accession
Q92598
Residue number A
140
Residue number B
167
Peptide name
Heat shock protein 105 kDa
Ligandability
Cysteine 140 of Heat shock protein 105 kDa
Cysteine 167 of Heat shock protein 105 kDa
6gfa A 166 A 379
A redox-regulated disulphide may form within Heat shock protein 105 kDa between cysteines 167 and 380 (166 and 379 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
6gfa
Structure name
structure of nucleotide binding domain of hsp110, atp and mg2+ complexed
Structure deposition date
2018-04-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
7
% buried
33
Peptide accession
Q92598
Residue number A
167
Residue number B
380
Peptide name
Heat shock protein 105 kDa
Ligandability
Cysteine 167 of Heat shock protein 105 kDa
Cysteine 380 of Heat shock protein 105 kDa
6gfa A 166 A 375
A redox-regulated disulphide may form within Heat shock protein 105 kDa between cysteines 167 and 376 (166 and 375 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
6gfa
Structure name
structure of nucleotide binding domain of hsp110, atp and mg2+ complexed
Structure deposition date
2018-04-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
7
% buried
83
Peptide accession
Q92598
Residue number A
167
Residue number B
376
Peptide name
Heat shock protein 105 kDa
Ligandability
Cysteine 167 of Heat shock protein 105 kDa
Cysteine 376 of Heat shock protein 105 kDa
6gfa A 139 A 379
A redox-regulated disulphide may form within Heat shock protein 105 kDa between cysteines 140 and 380 (139 and 379 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6gfa
Structure name
structure of nucleotide binding domain of hsp110, atp and mg2+ complexed
Structure deposition date
2018-04-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
36
Peptide accession
Q92598
Residue number A
140
Residue number B
380
Peptide name
Heat shock protein 105 kDa
Ligandability
Cysteine 140 of Heat shock protein 105 kDa
Cysteine 380 of Heat shock protein 105 kDa
6gfa A 375 A 379
A redox-regulated disulphide may form within Heat shock protein 105 kDa between cysteines 376 and 380 (375 and 379 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
6gfa
Structure name
structure of nucleotide binding domain of hsp110, atp and mg2+ complexed
Structure deposition date
2018-04-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
50
Peptide accession
Q92598
Residue number A
376
Residue number B
380
Peptide name
Heat shock protein 105 kDa
Ligandability
Cysteine 376 of Heat shock protein 105 kDa
Cysteine 380 of Heat shock protein 105 kDa
6gfa A 244 A 269
A redox-regulated disulphide may form within Heat shock protein 105 kDa between cysteines 245 and 270 (244 and 269 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
6gfa
Structure name
structure of nucleotide binding domain of hsp110, atp and mg2+ complexed
Structure deposition date
2018-04-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
64
Peptide accession
Q92598
Residue number A
245
Residue number B
270
Peptide name
Heat shock protein 105 kDa
Ligandability
Cysteine 245 of Heat shock protein 105 kDa
Cysteine 270 of Heat shock protein 105 kDa
6gfa A 12 A 33
A redox-regulated disulphide may form within Heat shock protein 105 kDa between cysteines 13 and 34 (12 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6gfa
Structure name
structure of nucleotide binding domain of hsp110, atp and mg2+ complexed
Structure deposition date
2018-04-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
86
Peptide accession
Q92598
Residue number A
13
Residue number B
34
Peptide name
Heat shock protein 105 kDa
Ligandability
Cysteine 13 of Heat shock protein 105 kDa
Cysteine 34 of Heat shock protein 105 kDa
6gfa A 139 A 375
A redox-regulated disulphide may form within Heat shock protein 105 kDa between cysteines 140 and 376 (139 and 375 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
6gfa
Structure name
structure of nucleotide binding domain of hsp110, atp and mg2+ complexed
Structure deposition date
2018-04-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
14
% buried
86
Peptide accession
Q92598
Residue number A
140
Residue number B
376
Peptide name
Heat shock protein 105 kDa
Ligandability
Cysteine 140 of Heat shock protein 105 kDa
Cysteine 376 of Heat shock protein 105 kDa
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