Protein transport protein Sec23A
Intramolecular
Cysteine 61 and cysteine 85 L
Cysteine 66 and cysteine 85
Cysteine 61 and cysteine 88 L
Cysteine 66 and cysteine 88
Cysteine 61 and cysteine 66 L
Cysteine 74 and cysteine 85
Cysteine 85 and cysteine 88
Cysteine 432 and cysteine 444
Cysteine 362 and cysteine 363
Cysteine 66 and cysteine 432
More...Cysteine 61 and cysteine 74 L
Cysteine 74 and cysteine 88
Cysteine 66 and cysteine 74
Cysteine 88 and cysteine 432
Cysteine 85 and cysteine 432
Cysteine 423 and cysteine 449
5vnk A 61 A 85
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 61 and 85.
Details
Redox score ?
91
PDB code
5vnk
Structure name
crystal structure of sec23a/sec24a/sec22 complexed with a c-terminal ll sorting motif
Structure deposition date
2017-04-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
4
% buried
42
Peptide accession
Q15436
Residue number A
61
Residue number B
85
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 61 of Protein transport protein Sec23A
Cysteine 85 of Protein transport protein Sec23A
5kyy A 66 A 85
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 66 and 85.
Details
Redox score ?
90
PDB code
5kyy
Structure name
crystal structure of sec23 and tango1 peptide4 complex
Structure deposition date
2016-07-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
4
% buried
55
Peptide accession
Q15436
Residue number A
66
Residue number B
85
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 66 of Protein transport protein Sec23A
Cysteine 85 of Protein transport protein Sec23A
5vnf A 61 A 88
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 61 and 88.
Details
Redox score ?
82
PDB code
5vnf
Structure name
crystal structure of sec23a/sec24a/sec22 complexed with a c-terminal vv sorting motif
Structure deposition date
2017-04-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
27
Peptide accession
Q15436
Residue number A
61
Residue number B
88
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 61 of Protein transport protein Sec23A
Cysteine 88 of Protein transport protein Sec23A
5vnn A 66 A 88
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 66 and 88.
Details
Redox score ?
82
PDB code
5vnn
Structure name
crystal structure of sec23a/sec24a/sec22 complexed with 4- phenylbutyric acid (50mm soaking)
Structure deposition date
2017-05-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
38
Peptide accession
Q15436
Residue number A
66
Residue number B
88
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 66 of Protein transport protein Sec23A
Cysteine 88 of Protein transport protein Sec23A
5vnk A 61 A 66
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 61 and 66.
Details
Redox score ?
79
PDB code
5vnk
Structure name
crystal structure of sec23a/sec24a/sec22 complexed with a c-terminal ll sorting motif
Structure deposition date
2017-04-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
39
Peptide accession
Q15436
Residue number A
61
Residue number B
66
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 61 of Protein transport protein Sec23A
Cysteine 66 of Protein transport protein Sec23A
5kyu A 74 A 85
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 74 and 85.
Details
Redox score ?
76
PDB code
5kyu
Structure name
crystal structure of sec23 and tango1 peptide2 complex
Structure deposition date
2016-07-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
4
% buried
75
Peptide accession
Q15436
Residue number A
74
Residue number B
85
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 74 of Protein transport protein Sec23A
Cysteine 85 of Protein transport protein Sec23A
5kyy A 85 A 88
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 85 and 88.
Details
Redox score ?
76
PDB code
5kyy
Structure name
crystal structure of sec23 and tango1 peptide4 complex
Structure deposition date
2016-07-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
43
Peptide accession
Q15436
Residue number A
85
Residue number B
88
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 85 of Protein transport protein Sec23A
Cysteine 88 of Protein transport protein Sec23A
5vnn A 432 A 444
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 432 and 444.
Details
Redox score ?
75
PDB code
5vnn
Structure name
crystal structure of sec23a/sec24a/sec22 complexed with 4- phenylbutyric acid (50mm soaking)
Structure deposition date
2017-05-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
6
% buried
64
Peptide accession
Q15436
Residue number A
432
Residue number B
444
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 432 of Protein transport protein Sec23A
Cysteine 444 of Protein transport protein Sec23A
5kyn A 362 A 363
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 362 and 363.
Details
Redox score ?
62
PDB code
5kyn
Structure name
structure of sec23 and tango1 complex
Structure deposition date
2016-07-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
88
Minimum pKa ?
8
% buried
95
Peptide accession
Q15436
Residue number A
362
Residue number B
363
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 362 of Protein transport protein Sec23A
Cysteine 363 of Protein transport protein Sec23A
2nup A 66 A 432
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 66 and 432. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
2nup
Structure name
crystal structure of the human sec23a/24a heterodimer, complexed with the snare protein sec22b
Structure deposition date
2006-11-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
58
Peptide accession
Q15436
Residue number A
66
Residue number B
432
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 66 of Protein transport protein Sec23A
Cysteine 432 of Protein transport protein Sec23A
5kyx A 61 A 74
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 61 and 74. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5kyx
Structure name
crystal structure of sec23 and tango1 peptide1 complex
Structure deposition date
2016-07-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
60
Peptide accession
Q15436
Residue number A
61
Residue number B
74
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 61 of Protein transport protein Sec23A
Cysteine 74 of Protein transport protein Sec23A
3egx A 74 A 88
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 74 and 88. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3egx
Structure name
crystal structure of the mammalian copii-coat protein sec23a/24a complexed with the snare protein sec22b and bound to the transport signal sequence of the snare protein bet1
Structure deposition date
2008-09-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
50
Peptide accession
Q15436
Residue number A
74
Residue number B
88
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 74 of Protein transport protein Sec23A
Cysteine 88 of Protein transport protein Sec23A
5vnf A 66 A 74
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 66 and 74. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5vnf
Structure name
crystal structure of sec23a/sec24a/sec22 complexed with a c-terminal vv sorting motif
Structure deposition date
2017-04-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
65
Peptide accession
Q15436
Residue number A
66
Residue number B
74
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 66 of Protein transport protein Sec23A
Cysteine 74 of Protein transport protein Sec23A
5kyy A 88 A 432
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 88 and 432. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5kyy
Structure name
crystal structure of sec23 and tango1 peptide4 complex
Structure deposition date
2016-07-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
55
Peptide accession
Q15436
Residue number A
88
Residue number B
432
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 88 of Protein transport protein Sec23A
Cysteine 432 of Protein transport protein Sec23A
5kyy A 85 A 432
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 85 and 432. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5kyy
Structure name
crystal structure of sec23 and tango1 peptide4 complex
Structure deposition date
2016-07-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
70
Peptide accession
Q15436
Residue number A
85
Residue number B
432
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 85 of Protein transport protein Sec23A
Cysteine 432 of Protein transport protein Sec23A
2nut A 423 A 449
A redox-regulated disulphide may form within Protein transport protein Sec23A between cysteines 423 and 449. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
22
PDB code
2nut
Structure name
crystal structure of the human sec23a/24a heterodimer, complexed with the snare protein sec22b
Structure deposition date
2006-11-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
99
Minimum pKa ?
12
% buried
99
Peptide accession
Q15436
Residue number A
423
Residue number B
449
Peptide name
Protein transport protein Sec23A
Ligandability
Cysteine 423 of Protein transport protein Sec23A
Cysteine 449 of Protein transport protein Sec23A
If this tool was useful for finding a disulphide, please cite: