Receptor-type tyrosine-protein phosphatase F
Intramolecular
Cysteine 54 and cysteine 107
Cysteine 156 and cysteine 207
Cysteine 1460 and cysteine 1548
Cysteine 1548 and cysteine 1557
Cysteine 1749 and cysteine 1839
3pxh A 54 A 107
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase F between cysteines 54 and 107.
Details
Redox score ?
81
PDB code
3pxh
Structure name
tandem ig domains of tyrosine phosphatase lar
Structure deposition date
2010-12-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2A8L5
Residue number A
54
Residue number B
107
Peptide name
Receptor-type tyrosine-protein phosphatase F
Ligandability
Cysteine 54 of Receptor-type tyrosine-protein phosphatase F
Cysteine 107 of Receptor-type tyrosine-protein phosphatase F
3pxh A 156 A 207
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase F between cysteines 156 and 207.
Details
Redox score ?
81
PDB code
3pxh
Structure name
tandem ig domains of tyrosine phosphatase lar
Structure deposition date
2010-12-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2A8L5
Residue number A
156
Residue number B
207
Peptide name
Receptor-type tyrosine-protein phosphatase F
Ligandability
Cysteine 156 of Receptor-type tyrosine-protein phosphatase F
Cysteine 207 of Receptor-type tyrosine-protein phosphatase F
6kr4 C 1460 C 1548
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase F between cysteines 1460 and 1548. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
6kr4
Structure name
crystal structure of the liprin-alpha3_sam123/lar_d1d2 complex
Structure deposition date
2019-08-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
99
Peptide accession
P10586
Residue number A
1460
Residue number B
1548
Peptide name
Receptor-type tyrosine-protein phosphatase F
Ligandability
Cysteine 1460 of Receptor-type tyrosine-protein phosphatase F
Cysteine 1548 of Receptor-type tyrosine-protein phosphatase F
1lar B 1522 B 1531
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase F between cysteines 1548 and 1557 (1522 and 1531 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
1lar
Structure name
crystal structure of the tandem phosphatase domains of rptp lar
Structure deposition date
1999-04-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
8
% buried
100
Peptide accession
P10586
Residue number A
1548
Residue number B
1557
Peptide name
Receptor-type tyrosine-protein phosphatase F
Ligandability
Cysteine 1548 of Receptor-type tyrosine-protein phosphatase F
Cysteine 1557 of Receptor-type tyrosine-protein phosphatase F
6kr4 A 1749 A 1839
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase F between cysteines 1749 and 1839. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
6kr4
Structure name
crystal structure of the liprin-alpha3_sam123/lar_d1d2 complex
Structure deposition date
2019-08-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
98
Peptide accession
P10586
Residue number A
1749
Residue number B
1839
Peptide name
Receptor-type tyrosine-protein phosphatase F
Ligandability
Cysteine 1749 of Receptor-type tyrosine-protein phosphatase F
Cysteine 1839 of Receptor-type tyrosine-protein phosphatase F
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