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Protein transport protein Sec24C

Intramolecular
Cysteine 425 and cysteine 450
Cysteine 428 and cysteine 447
Cysteine 447 and cysteine 450
Cysteine 428 and cysteine 450
Cysteine 450 and cysteine 452
Cysteine 433 and cysteine 448 L
Cysteine 383 and cysteine 831 L
Cysteine 687 and cysteine 692
Cysteine 425 and cysteine 428
Cysteine 447 and cysteine 452
More...
Cysteine 842 and cysteine 900 L
Cysteine 881 and cysteine 886 L
Cysteine 383 and cysteine 832 L
Cysteine 448 and cysteine 450
Cysteine 428 and cysteine 452
Cysteine 433 and cysteine 447 L
Cysteine 428 and cysteine 433 L
Cysteine 425 and cysteine 452
Cysteine 425 and cysteine 448
Cysteine 831 and cysteine 832 L
Cysteine 447 and cysteine 448
Cysteine 832 and cysteine 886 L
Cysteine 425 and cysteine 447
Cysteine 687 and cysteine 693
Cysteine 832 and cysteine 842 L
Cysteine 428 and cysteine 448
Cysteine 692 and cysteine 693
Cysteine 635 and cysteine 692 L
A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 425 and 450 (98 and 123 respectively in this structure).

Details

Redox score ?
90
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
0
% buried
nan
Peptide accession
P53992
Residue number A
425
Residue number B
450
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 425 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 450 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 428 and 447 (101 and 120 respectively in this structure).

Details

Redox score ?
85
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
4
% buried
56
Peptide accession
P53992
Residue number A
428
Residue number B
447
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 428 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 447 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 447 and 450 (120 and 123 respectively in this structure).

Details

Redox score ?
71
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
36
Peptide accession
P53992
Residue number A
447
Residue number B
450
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 447 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 450 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 428 and 450 (101 and 123 respectively in this structure).

Details

Redox score ?
70
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
40
Peptide accession
P53992
Residue number A
428
Residue number B
450
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 428 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 450 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 450 and 452 (123 and 125 respectively in this structure).

Details

Redox score ?
69
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
10
Peptide accession
P53992
Residue number A
450
Residue number B
452
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 450 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 452 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 433 and 448 (106 and 121 respectively in this structure).

Details

Redox score ?
68
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
8
% buried
100
Peptide accession
P53992
Residue number A
433
Residue number B
448
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 433 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 448 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 383 and 831 (56 and 504 respectively in this structure).

Details

Redox score ?
67
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
44
Peptide accession
P53992
Residue number A
383
Residue number B
831
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 383 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 831 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 687 and 692 (360 and 365 respectively in this structure).

Details

Redox score ?
66
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
94
Minimum pKa ?
9
% buried
99
Peptide accession
P53992
Residue number A
687
Residue number B
692
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 687 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 692 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 425 and 428 (98 and 101 respectively in this structure).

Details

Redox score ?
61
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
14
% buried
nan
Peptide accession
P53992
Residue number A
425
Residue number B
428
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 425 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 428 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 447 and 452 (120 and 125 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
26
Peptide accession
P53992
Residue number A
447
Residue number B
452
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 447 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 452 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 842 and 900 (515 and 573 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
90
Peptide accession
P53992
Residue number A
842
Residue number B
900
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 842 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 900 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 881 and 886 (554 and 559 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
30
Peptide accession
P53992
Residue number A
881
Residue number B
886
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 881 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 886 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 383 and 832 (56 and 505 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
44
Peptide accession
P53992
Residue number A
383
Residue number B
832
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 383 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 832 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 448 and 450 (121 and 123 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
0
% buried
100
Peptide accession
P53992
Residue number A
448
Residue number B
450
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 448 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 450 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 428 and 452 (101 and 125 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
26
Peptide accession
P53992
Residue number A
428
Residue number B
452
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 428 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 452 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 433 and 447 (106 and 120 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
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
96
Peptide accession
P53992
Residue number A
433
Residue number B
447
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 433 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 447 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 428 and 433 (101 and 106 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
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
4
% buried
74
Peptide accession
P53992
Residue number A
428
Residue number B
433
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 428 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 433 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 425 and 452 (98 and 125 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
18
% buried
nan
Peptide accession
P53992
Residue number A
425
Residue number B
452
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 425 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 452 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 425 and 448 (98 and 121 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
64
Peptide accession
P53992
Residue number A
425
Residue number B
448
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 425 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 448 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 831 and 832 (504 and 505 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
62
Peptide accession
P53992
Residue number A
831
Residue number B
832
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 831 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 832 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 447 and 448 (120 and 121 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
18
% buried
96
Peptide accession
P53992
Residue number A
447
Residue number B
448
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 447 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 448 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 832 and 886 (505 and 559 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
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
38
Peptide accession
P53992
Residue number A
832
Residue number B
886
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 832 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 886 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 425 and 447 (98 and 120 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
25
% buried
nan
Peptide accession
P53992
Residue number A
425
Residue number B
447
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 425 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 447 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 687 and 693 (360 and 366 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
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
9
% buried
98
Peptide accession
P53992
Residue number A
687
Residue number B
693
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 687 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 693 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 832 and 842 (505 and 515 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
80
Peptide accession
P53992
Residue number A
832
Residue number B
842
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 832 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 842 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 428 and 448 (101 and 121 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
14
% buried
100
Peptide accession
P53992
Residue number A
428
Residue number B
448
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 428 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 448 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 692 and 693 (365 and 366 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
102
Minimum pKa ?
12
% buried
100
Peptide accession
P53992
Residue number A
692
Residue number B
693
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 692 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 693 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein transport protein Sec24C between cysteines 635 and 692 (308 and 365 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
3eh2
Structure name
crystal structure of the human copii-coat protein sec24c
Structure deposition date
2008-09-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
88
Peptide accession
P53992
Residue number A
635
Residue number B
692
Peptide name
Protein transport protein Sec24C

Ligandability

Cysteine 635 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 692 of Protein transport protein Sec24C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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