Angiopoietin-1
Intramolecular
Cysteine 435 and cysteine 437
Cysteine 439 and cysteine 452
Cysteine 286 and cysteine 315
Cysteine 437 and cysteine 452
Cysteine 435 and cysteine 439
Cysteine 437 and cysteine 439
Cysteine 435 and cysteine 452
4epu B 435 B 437
A redox-regulated disulphide may form within Angiopoietin-1 between cysteines 435 and 437.
Details
Redox score ?
86
PDB code
4epu
Structure name
ang1 fibrinogen-related domain (fred)
Structure deposition date
2012-04-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15389
Residue number A
435
Residue number B
437
Peptide name
Angiopoietin-1
Ligandability
Cysteine 435 of Angiopoietin-1
Cysteine 437 of Angiopoietin-1
4epu A 439 A 452
A redox-regulated disulphide may form within Angiopoietin-1 between cysteines 439 and 452.
Details
Redox score ?
83
PDB code
4epu
Structure name
ang1 fibrinogen-related domain (fred)
Structure deposition date
2012-04-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15389
Residue number A
439
Residue number B
452
Peptide name
Angiopoietin-1
Ligandability
Cysteine 439 of Angiopoietin-1
Cysteine 452 of Angiopoietin-1
4epu A 286 A 315
A redox-regulated disulphide may form within Angiopoietin-1 between cysteines 286 and 315.
Details
Redox score ?
83
PDB code
4epu
Structure name
ang1 fibrinogen-related domain (fred)
Structure deposition date
2012-04-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15389
Residue number A
286
Residue number B
315
Peptide name
Angiopoietin-1
Ligandability
Cysteine 286 of Angiopoietin-1
Cysteine 315 of Angiopoietin-1
4epu A 437 A 452
A redox-regulated disulphide may form within Angiopoietin-1 between cysteines 437 and 452.
Details
Redox score ?
73
PDB code
4epu
Structure name
ang1 fibrinogen-related domain (fred)
Structure deposition date
2012-04-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15389
Residue number A
437
Residue number B
452
Peptide name
Angiopoietin-1
Ligandability
Cysteine 437 of Angiopoietin-1
Cysteine 452 of Angiopoietin-1
4epu B 435 B 439
A redox-regulated disulphide may form within Angiopoietin-1 between cysteines 435 and 439.
Details
Redox score ?
73
PDB code
4epu
Structure name
ang1 fibrinogen-related domain (fred)
Structure deposition date
2012-04-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15389
Residue number A
435
Residue number B
439
Peptide name
Angiopoietin-1
Ligandability
Cysteine 435 of Angiopoietin-1
Cysteine 439 of Angiopoietin-1
4epu A 437 A 439
A redox-regulated disulphide may form within Angiopoietin-1 between cysteines 437 and 439.
Details
Redox score ?
72
PDB code
4epu
Structure name
ang1 fibrinogen-related domain (fred)
Structure deposition date
2012-04-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15389
Residue number A
437
Residue number B
439
Peptide name
Angiopoietin-1
Ligandability
Cysteine 437 of Angiopoietin-1
Cysteine 439 of Angiopoietin-1
4jyo X 156 X 173
A redox-regulated disulphide may form within Angiopoietin-1 between cysteines 435 and 452 (156 and 173 respectively in this structure).
Details
Redox score ?
70
PDB code
4jyo
Structure name
structural basis for angiopoietin-1 mediated signaling initiation
Structure deposition date
2013-03-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15389
Residue number A
435
Residue number B
452
Peptide name
Angiopoietin-1
Ligandability
Cysteine 435 of Angiopoietin-1
Cysteine 452 of Angiopoietin-1
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