Actin-related protein 8
Intramolecular
Cysteine 293 and cysteine 522
Cysteine 280 and cysteine 293
Cysteine 521 and cysteine 522
Cysteine 332 and cysteine 340
Cysteine 280 and cysteine 522
Cysteine 280 and cysteine 292
Cysteine 293 and cysteine 521
Cysteine 317 and cysteine 351
Cysteine 292 and cysteine 293
Cysteine 292 and cysteine 522
4fo0 A 293 A 522
A redox-regulated disulphide may form within Actin-related protein 8 between cysteines 293 and 522.
Details
Redox score ?
62
PDB code
4fo0
Structure name
human actin-related protein arp8 in its atp-bound state
Structure deposition date
2012-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
14
% buried
74
Peptide accession
Q9H981
Residue number A
293
Residue number B
522
Peptide name
Actin-related protein 8
Ligandability
Cysteine 293 of Actin-related protein 8
Cysteine 522 of Actin-related protein 8
4fo0 A 280 A 293
A redox-regulated disulphide may form within Actin-related protein 8 between cysteines 280 and 293.
Details
Redox score ?
60
PDB code
4fo0
Structure name
human actin-related protein arp8 in its atp-bound state
Structure deposition date
2012-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
100
Minimum pKa ?
10
% buried
98
Peptide accession
Q9H981
Residue number A
280
Residue number B
293
Peptide name
Actin-related protein 8
Ligandability
Cysteine 280 of Actin-related protein 8
Cysteine 293 of Actin-related protein 8
4fo0 A 521 A 522
A redox-regulated disulphide may form within Actin-related protein 8 between cysteines 521 and 522. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
4fo0
Structure name
human actin-related protein arp8 in its atp-bound state
Structure deposition date
2012-06-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
42
Peptide accession
Q9H981
Residue number A
521
Residue number B
522
Peptide name
Actin-related protein 8
Ligandability
Cysteine 521 of Actin-related protein 8
Cysteine 522 of Actin-related protein 8
4fo0 A 332 A 340
A redox-regulated disulphide may form within Actin-related protein 8 between cysteines 332 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
4fo0
Structure name
human actin-related protein arp8 in its atp-bound state
Structure deposition date
2012-06-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
13
% buried
86
Peptide accession
Q9H981
Residue number A
332
Residue number B
340
Peptide name
Actin-related protein 8
Ligandability
Cysteine 332 of Actin-related protein 8
Cysteine 340 of Actin-related protein 8
4fo0 A 280 A 522
A redox-regulated disulphide may form within Actin-related protein 8 between cysteines 280 and 522. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
4fo0
Structure name
human actin-related protein arp8 in its atp-bound state
Structure deposition date
2012-06-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
10
% buried
76
Peptide accession
Q9H981
Residue number A
280
Residue number B
522
Peptide name
Actin-related protein 8
Ligandability
Cysteine 280 of Actin-related protein 8
Cysteine 522 of Actin-related protein 8
4fo0 A 280 A 292
A redox-regulated disulphide may form within Actin-related protein 8 between cysteines 280 and 292. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
4fo0
Structure name
human actin-related protein arp8 in its atp-bound state
Structure deposition date
2012-06-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
104
Minimum pKa ?
10
% buried
100
Peptide accession
Q9H981
Residue number A
280
Residue number B
292
Peptide name
Actin-related protein 8
Ligandability
Cysteine 280 of Actin-related protein 8
Cysteine 292 of Actin-related protein 8
4fo0 A 293 A 521
A redox-regulated disulphide may form within Actin-related protein 8 between cysteines 293 and 521. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
4fo0
Structure name
human actin-related protein arp8 in its atp-bound state
Structure deposition date
2012-06-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
65
Peptide accession
Q9H981
Residue number A
293
Residue number B
521
Peptide name
Actin-related protein 8
Ligandability
Cysteine 293 of Actin-related protein 8
Cysteine 521 of Actin-related protein 8
4fo0 A 317 A 351
A redox-regulated disulphide may form within Actin-related protein 8 between cysteines 317 and 351. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
4fo0
Structure name
human actin-related protein arp8 in its atp-bound state
Structure deposition date
2012-06-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
100
Peptide accession
Q9H981
Residue number A
317
Residue number B
351
Peptide name
Actin-related protein 8
Ligandability
Cysteine 317 of Actin-related protein 8
Cysteine 351 of Actin-related protein 8
4fo0 A 292 A 293
A redox-regulated disulphide may form within Actin-related protein 8 between cysteines 292 and 293. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
4fo0
Structure name
human actin-related protein arp8 in its atp-bound state
Structure deposition date
2012-06-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
102
Minimum pKa ?
14
% buried
98
Peptide accession
Q9H981
Residue number A
292
Residue number B
293
Peptide name
Actin-related protein 8
Ligandability
Cysteine 292 of Actin-related protein 8
Cysteine 293 of Actin-related protein 8
4fo0 A 292 A 522
A redox-regulated disulphide may form within Actin-related protein 8 between cysteines 292 and 522. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
4fo0
Structure name
human actin-related protein arp8 in its atp-bound state
Structure deposition date
2012-06-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
14
% buried
76
Peptide accession
Q9H981
Residue number A
292
Residue number B
522
Peptide name
Actin-related protein 8
Ligandability
Cysteine 292 of Actin-related protein 8
Cysteine 522 of Actin-related protein 8
If this tool was useful for finding a disulphide, please cite: