Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Intramolecular
Cysteine 459 and cysteine 462
Cysteine 442 and cysteine 459
Cysteine 439 and cysteine 459
Cysteine 439 and cysteine 442
Cysteine 442 and cysteine 462
Cysteine 506 and cysteine 507
Cysteine 439 and cysteine 462
Cysteine 632 and cysteine 672
Cysteine 631 and cysteine 672
Cysteine 631 and cysteine 639
More...Cysteine 439 and cysteine 440
Cysteine 631 and cysteine 632
Cysteine 639 and cysteine 672
Cysteine 440 and cysteine 442
Cysteine 440 and cysteine 462
1dcq A 284 A 287
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 459 and 462 (284 and 287 respectively in this structure).
Details
Redox score ?
87
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
79
Minimum pKa ?
2
% buried
60
Peptide accession
Q7SIG6
Residue number A
459
Residue number B
462
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 459 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 462 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 267 A 284
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 442 and 459 (267 and 284 respectively in this structure).
Details
Redox score ?
86
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
2
% buried
43
Peptide accession
Q7SIG6
Residue number A
442
Residue number B
459
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 442 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 459 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 264 A 284
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 439 and 459 (264 and 284 respectively in this structure).
Details
Redox score ?
84
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
2
% buried
66
Peptide accession
Q7SIG6
Residue number A
439
Residue number B
459
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 439 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 459 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 264 A 267
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 439 and 442 (264 and 267 respectively in this structure).
Details
Redox score ?
75
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
60
Peptide accession
Q7SIG6
Residue number A
439
Residue number B
442
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 439 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 442 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 267 A 287
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 442 and 462 (267 and 287 respectively in this structure).
Details
Redox score ?
74
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
8
% buried
54
Peptide accession
Q7SIG6
Residue number A
442
Residue number B
462
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 442 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 462 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 331 A 332
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 506 and 507 (331 and 332 respectively in this structure).
Details
Redox score ?
74
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
2
Peptide accession
Q7SIG6
Residue number A
506
Residue number B
507
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 506 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 507 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 264 A 287
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 439 and 462 (264 and 287 respectively in this structure).
Details
Redox score ?
73
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
76
Peptide accession
Q7SIG6
Residue number A
439
Residue number B
462
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 439 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 462 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 457 A 497
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 632 and 672 (457 and 497 respectively in this structure).
Details
Redox score ?
70
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
64
Peptide accession
Q7SIG6
Residue number A
632
Residue number B
672
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 632 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 672 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 456 A 497
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 631 and 672 (456 and 497 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
8
% buried
76
Peptide accession
Q7SIG6
Residue number A
631
Residue number B
672
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 631 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 672 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 456 A 464
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 631 and 639 (456 and 464 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
Q7SIG6
Residue number A
631
Residue number B
639
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 631 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 639 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 264 A 265
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 439 and 440 (264 and 265 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
9
% buried
91
Peptide accession
Q7SIG6
Residue number A
439
Residue number B
440
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 439 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 440 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 456 A 457
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 631 and 632 (456 and 457 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
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
15
% buried
87
Peptide accession
Q7SIG6
Residue number A
631
Residue number B
632
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 631 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 632 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 464 A 497
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 639 and 672 (464 and 497 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
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
8
% buried
76
Peptide accession
Q7SIG6
Residue number A
639
Residue number B
672
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 639 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 672 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 265 A 267
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 440 and 442 (265 and 267 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
8
% buried
68
Peptide accession
Q7SIG6
Residue number A
440
Residue number B
442
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 440 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 442 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
1dcq A 265 A 287
A redox-regulated disulphide may form within Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 between cysteines 440 and 462 (265 and 287 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
1dcq
Structure name
crystal structure of the arf-gap domain and ankyrin repeats of papbeta
Structure deposition date
1999-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
86
Peptide accession
Q7SIG6
Residue number A
440
Residue number B
462
Peptide name
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Ligandability
Cysteine 440 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Cysteine 462 of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
If this tool was useful for finding a disulphide, please cite: