Cryptochrome-1
Intermolecular
Cysteine 414 and cysteine 1210 of Period circadian protein homolog 2
Cysteine 414 and cysteine 1213 of Period circadian protein homolog 2
Cysteine 412 and cysteine 1210 of Period circadian protein homolog 2
Cysteine 363 and cysteine 1210 of Period circadian protein homolog 2
Intramolecular
Cysteine 363 and cysteine 412
Cysteine 58 and cysteine 259
Cysteine 412 and cysteine 414
Cysteine 24 and cysteine 178
Cysteine 363 and cysteine 402
Cysteine 24 and cysteine 33
More...Cysteine 33 and cysteine 178
Cysteine 402 and cysteine 412
Cysteine 363 and cysteine 414
4ct0 A 414 B 1210
A redox-regulated disulphide may form between cysteine 414 of Cryptochrome-1 and cysteine 1210 of Period circadian protein homolog 2.
Details
Redox score ?
88
PDB code
4ct0
Structure name
crystal structure of mouse cryptochrome1 in complex with period2
Structure deposition date
2014-03-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
74
Minimum pKa ?
2
% buried
66
Peptide A name
Cryptochrome-1
Peptide B name
Period circadian protein homolog 2
Peptide A accession
P97784
Peptide B accession
O54943
Peptide A residue number
414
Peptide B residue number
1210
Ligandability
Cysteine 414 of Cryptochrome-1
Cysteine 1210 of Period circadian protein homolog 2
4ct0 A 414 B 1213
A redox-regulated disulphide may form between cysteine 414 of Cryptochrome-1 and cysteine 1213 of Period circadian protein homolog 2.
Details
Redox score ?
75
PDB code
4ct0
Structure name
crystal structure of mouse cryptochrome1 in complex with period2
Structure deposition date
2014-03-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
57
Peptide A name
Cryptochrome-1
Peptide B name
Period circadian protein homolog 2
Peptide A accession
P97784
Peptide B accession
O54943
Peptide A residue number
414
Peptide B residue number
1213
Ligandability
Cysteine 414 of Cryptochrome-1
Cysteine 1213 of Period circadian protein homolog 2
4ct0 A 412 B 1210
A redox-regulated disulphide may form between cysteine 412 of Cryptochrome-1 and cysteine 1210 of Period circadian protein homolog 2.
Details
Redox score ?
66
PDB code
4ct0
Structure name
crystal structure of mouse cryptochrome1 in complex with period2
Structure deposition date
2014-03-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
2
% buried
78
Peptide A name
Cryptochrome-1
Peptide B name
Period circadian protein homolog 2
Peptide A accession
P97784
Peptide B accession
O54943
Peptide A residue number
412
Peptide B residue number
1210
Ligandability
Cysteine 412 of Cryptochrome-1
Cysteine 1210 of Period circadian protein homolog 2
4ct0 A 363 B 1210
A redox-regulated disulphide may form between cysteine 363 of Cryptochrome-1 and cysteine 1210 of Period circadian protein homolog 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
4ct0
Structure name
crystal structure of mouse cryptochrome1 in complex with period2
Structure deposition date
2014-03-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
2
% buried
78
Peptide A name
Cryptochrome-1
Peptide B name
Period circadian protein homolog 2
Peptide A accession
P97784
Peptide B accession
O54943
Peptide A residue number
363
Peptide B residue number
1210
Ligandability
Cysteine 363 of Cryptochrome-1
Cysteine 1210 of Period circadian protein homolog 2
7d0m A 363 A 412
A redox-regulated disulphide may form within Cryptochrome-1 between cysteines 363 and 412.
Details
Redox score ?
73
PDB code
7d0m
Structure name
crystal structure of mouse cry1 with bound cryoprotectant
Structure deposition date
2020-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
77
Peptide accession
P97784
Residue number A
363
Residue number B
412
Peptide name
Cryptochrome-1
Ligandability
Cysteine 363 of Cryptochrome-1
Cysteine 412 of Cryptochrome-1
5t5x A 58 A 259
A redox-regulated disulphide may form within Cryptochrome-1 between cysteines 58 and 259.
Details
Redox score ?
70
PDB code
5t5x
Structure name
high resolution structure of mouse cryptochrome 1
Structure deposition date
2016-08-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
100
Peptide accession
P97784
Residue number A
58
Residue number B
259
Peptide name
Cryptochrome-1
Ligandability
Cysteine 58 of Cryptochrome-1
Cysteine 259 of Cryptochrome-1
7d19 A 412 A 414
A redox-regulated disulphide may form within Cryptochrome-1 between cysteines 412 and 414. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
7d19
Structure name
crystal structure of mouse cryptochrome 1 in complex with compound th129
Structure deposition date
2020-09-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
45
Peptide accession
P97784
Residue number A
412
Residue number B
414
Peptide name
Cryptochrome-1
Ligandability
Cysteine 412 of Cryptochrome-1
Cysteine 414 of Cryptochrome-1
7d19 B 24 B 178
A redox-regulated disulphide may form within Cryptochrome-1 between cysteines 24 and 178. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
7d19
Structure name
crystal structure of mouse cryptochrome 1 in complex with compound th129
Structure deposition date
2020-09-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
66
Peptide accession
P97784
Residue number A
24
Residue number B
178
Peptide name
Cryptochrome-1
Ligandability
Cysteine 24 of Cryptochrome-1
Cysteine 178 of Cryptochrome-1
7d0m A 363 A 402
A redox-regulated disulphide may form within Cryptochrome-1 between cysteines 363 and 402. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
7d0m
Structure name
crystal structure of mouse cry1 with bound cryoprotectant
Structure deposition date
2020-09-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
7
% buried
90
Peptide accession
P97784
Residue number A
363
Residue number B
402
Peptide name
Cryptochrome-1
Ligandability
Cysteine 363 of Cryptochrome-1
Cysteine 402 of Cryptochrome-1
6of7 A 24 A 33
A redox-regulated disulphide may form within Cryptochrome-1 between cysteines 24 and 33. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6of7
Structure name
crystal structure of the cry1-per2 complex
Structure deposition date
2019-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
89
Peptide accession
P97784
Residue number A
24
Residue number B
33
Peptide name
Cryptochrome-1
Ligandability
Cysteine 24 of Cryptochrome-1
Cysteine 33 of Cryptochrome-1
4ct0 A 33 A 178
A redox-regulated disulphide may form within Cryptochrome-1 between cysteines 33 and 178. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
4ct0
Structure name
crystal structure of mouse cryptochrome1 in complex with period2
Structure deposition date
2014-03-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
67
Peptide accession
P97784
Residue number A
33
Residue number B
178
Peptide name
Cryptochrome-1
Ligandability
Cysteine 33 of Cryptochrome-1
Cysteine 178 of Cryptochrome-1
7d19 B 402 B 412
A redox-regulated disulphide may form within Cryptochrome-1 between cysteines 402 and 412. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
7d19
Structure name
crystal structure of mouse cryptochrome 1 in complex with compound th129
Structure deposition date
2020-09-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
10
% buried
96
Peptide accession
P97784
Residue number A
402
Residue number B
412
Peptide name
Cryptochrome-1
Ligandability
Cysteine 402 of Cryptochrome-1
Cysteine 412 of Cryptochrome-1
7wva A 363 A 414
A redox-regulated disulphide may form within Cryptochrome-1 between cysteines 363 and 414. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
7wva
Structure name
crystal structure of mouse cryptochrome 1 in complex with th401 compound
Structure deposition date
2022-02-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
66
Peptide accession
P97784
Residue number A
363
Residue number B
414
Peptide name
Cryptochrome-1
Ligandability
Cysteine 363 of Cryptochrome-1
Cysteine 414 of Cryptochrome-1
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