Polycystin-2
Intramolecular
Cysteine 331 and cysteine 344
Cysteine 476 and cysteine 481
Cysteine 235 and cysteine 476
5mke B 331 B 344
A redox-regulated disulphide may form within Polycystin-2 between cysteines 331 and 344. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5mke
Structure name
cryoem structure of polycystin-2 in complex with cations and lipids
Structure deposition date
2016-12-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
48
Peptide accession
Q13563
Residue number A
331
Residue number B
344
Peptide name
Polycystin-2
Ligandability
Cysteine 331 of Polycystin-2
Cysteine 344 of Polycystin-2
5mkf C 476 C 481
A redox-regulated disulphide may form within Polycystin-2 between cysteines 476 and 481. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5mkf
Structure name
cryoem structure of polycystin-2 in complex with calcium and lipids
Structure deposition date
2016-12-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
10
% buried
20
Peptide accession
Q13563
Residue number A
476
Residue number B
481
Peptide name
Polycystin-2
Ligandability
Cysteine 476 of Polycystin-2
Cysteine 481 of Polycystin-2
6a70 F 235 F 476
A redox-regulated disulphide may form within Polycystin-2 between cysteines 235 and 476. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
6a70
Structure name
structure of the human pkd1/pkd2 complex
Structure deposition date
2018-06-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
32
Peptide accession
Q13563
Residue number A
235
Residue number B
476
Peptide name
Polycystin-2
Ligandability
Cysteine 235 of Polycystin-2
Cysteine 476 of Polycystin-2
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