Cryptochrome-2
Intermolecular
Cysteine 432 and cysteine 1210 of Period circadian protein homolog 2
Cysteine 430 and cysteine 340 of F-box/LRR-repeat protein 3
Cysteine 432 and cysteine 1213 of Period circadian protein homolog 2
Cysteine 430 and cysteine 1210 of Period circadian protein homolog 2
Cysteine 432 and cysteine 340 of F-box/LRR-repeat protein 3
Cysteine 430 and cysteine 1213 of Period circadian protein homolog 2
Cysteine 381 and cysteine 1210 of Period circadian protein homolog 2
Cysteine 381 and cysteine 340 of F-box/LRR-repeat protein 3
Intramolecular
Cysteine 381 and cysteine 430
Cysteine 48 and cysteine 196
More...Cysteine 430 and cysteine 432
Cysteine 51 and cysteine 196
Cysteine 381 and cysteine 420
Cysteine 48 and cysteine 51
Cysteine 381 and cysteine 432
Cysteine 420 and cysteine 430
4u8h A 432 B 1210
A redox-regulated disulphide may form between cysteine 432 of Cryptochrome-2 and cysteine 1210 of Period circadian protein homolog 2.
Details
Redox score ?
83
PDB code
4u8h
Structure name
crystal structure of mammalian period-cryptochrome complex
Structure deposition date
2014-08-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
1
% buried
71
Peptide A name
Cryptochrome-2
Peptide B name
Period circadian protein homolog 2
Peptide A accession
Q9R194
Peptide B accession
O54943
Peptide A residue number
432
Peptide B residue number
1210
Ligandability
Cysteine 432 of Cryptochrome-2
Cysteine 1210 of Period circadian protein homolog 2
4i6j A 430 B 340
A redox-regulated disulphide may form between cysteine 430 of Cryptochrome-2 and cysteine 340 of F-box/LRR-repeat protein 3.
Details
Redox score ?
77
PDB code
4i6j
Structure name
a ubiquitin ligase-substrate complex
Structure deposition date
2012-11-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide A name
Cryptochrome-2
Peptide B name
F-box/LRR-repeat protein 3
Peptide A accession
Q9R194
Peptide B accession
Q9UKT7
Peptide A residue number
430
Peptide B residue number
340
Ligandability
Cysteine 430 of Cryptochrome-2
Cysteine 340 of F-box/LRR-repeat protein 3
4u8h A 432 B 1213
A redox-regulated disulphide may form between cysteine 432 of Cryptochrome-2 and cysteine 1213 of Period circadian protein homolog 2.
Details
Redox score ?
69
PDB code
4u8h
Structure name
crystal structure of mammalian period-cryptochrome complex
Structure deposition date
2014-08-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
60
Peptide A name
Cryptochrome-2
Peptide B name
Period circadian protein homolog 2
Peptide A accession
Q9R194
Peptide B accession
O54943
Peptide A residue number
432
Peptide B residue number
1213
Ligandability
Cysteine 432 of Cryptochrome-2
Cysteine 1213 of Period circadian protein homolog 2
4u8h C 430 D 1210
A redox-regulated disulphide may form between cysteine 430 of Cryptochrome-2 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 ?
52
PDB code
4u8h
Structure name
crystal structure of mammalian period-cryptochrome complex
Structure deposition date
2014-08-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
nan
Peptide A name
Cryptochrome-2
Peptide B name
Period circadian protein homolog 2
Peptide A accession
Q9R194
Peptide B accession
O54943
Peptide A residue number
430
Peptide B residue number
1210
Ligandability
Cysteine 430 of Cryptochrome-2
Cysteine 1210 of Period circadian protein homolog 2
4i6j A 432 B 340
A redox-regulated disulphide may form between cysteine 432 of Cryptochrome-2 and cysteine 340 of F-box/LRR-repeat protein 3. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
4i6j
Structure name
a ubiquitin ligase-substrate complex
Structure deposition date
2012-11-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
87
Minimum pKa ?
5
% buried
nan
Peptide A name
Cryptochrome-2
Peptide B name
F-box/LRR-repeat protein 3
Peptide A accession
Q9R194
Peptide B accession
Q9UKT7
Peptide A residue number
432
Peptide B residue number
340
Ligandability
Cysteine 432 of Cryptochrome-2
Cysteine 340 of F-box/LRR-repeat protein 3
4u8h C 430 D 1213
A redox-regulated disulphide may form between cysteine 430 of Cryptochrome-2 and cysteine 1213 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 ?
46
PDB code
4u8h
Structure name
crystal structure of mammalian period-cryptochrome complex
Structure deposition date
2014-08-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide A name
Cryptochrome-2
Peptide B name
Period circadian protein homolog 2
Peptide A accession
Q9R194
Peptide B accession
O54943
Peptide A residue number
430
Peptide B residue number
1213
Ligandability
Cysteine 430 of Cryptochrome-2
Cysteine 1213 of Period circadian protein homolog 2
4u8h C 381 D 1210
A redox-regulated disulphide may form between cysteine 381 of Cryptochrome-2 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 ?
44
PDB code
4u8h
Structure name
crystal structure of mammalian period-cryptochrome complex
Structure deposition date
2014-08-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
nan
Peptide A name
Cryptochrome-2
Peptide B name
Period circadian protein homolog 2
Peptide A accession
Q9R194
Peptide B accession
O54943
Peptide A residue number
381
Peptide B residue number
1210
Ligandability
Cysteine 381 of Cryptochrome-2
Cysteine 1210 of Period circadian protein homolog 2
4i6j A 381 B 340
A redox-regulated disulphide may form between cysteine 381 of Cryptochrome-2 and cysteine 340 of F-box/LRR-repeat protein 3. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
4i6j
Structure name
a ubiquitin ligase-substrate complex
Structure deposition date
2012-11-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
nan
Peptide A name
Cryptochrome-2
Peptide B name
F-box/LRR-repeat protein 3
Peptide A accession
Q9R194
Peptide B accession
Q9UKT7
Peptide A residue number
381
Peptide B residue number
340
Ligandability
Cysteine 381 of Cryptochrome-2
Cysteine 340 of F-box/LRR-repeat protein 3
4mlp A 381 A 430
A redox-regulated disulphide may form within Cryptochrome-2 between cysteines 381 and 430.
Details
Redox score ?
78
PDB code
4mlp
Structure name
mammalian cryptochrome in complex with a small molecule competitor of its ubiquitin ligase
Structure deposition date
2013-09-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
100
Peptide accession
Q9R194
Residue number A
381
Residue number B
430
Peptide name
Cryptochrome-2
Ligandability
Cysteine 381 of Cryptochrome-2
Cysteine 430 of Cryptochrome-2
4i6e A 48 A 196
A redox-regulated disulphide may form within Cryptochrome-2 between cysteines 48 and 196. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
4i6e
Structure name
a vertebrate cryptochrome
Structure deposition date
2012-11-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
26
Peptide accession
Q9R194
Residue number A
48
Residue number B
196
Peptide name
Cryptochrome-2
Ligandability
Cysteine 48 of Cryptochrome-2
Cysteine 196 of Cryptochrome-2
7d0n A 430 A 432
A redox-regulated disulphide may form within Cryptochrome-2 between cysteines 430 and 432. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
7d0n
Structure name
crystal structure of mouse cry2 apo form
Structure deposition date
2020-09-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
32
Peptide accession
Q9R194
Residue number A
430
Residue number B
432
Peptide name
Cryptochrome-2
Ligandability
Cysteine 430 of Cryptochrome-2
Cysteine 432 of Cryptochrome-2
4i6g B 51 B 196
A redox-regulated disulphide may form within Cryptochrome-2 between cysteines 51 and 196. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
4i6g
Structure name
a vertebrate cryptochrome with fad
Structure deposition date
2012-11-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
72
Peptide accession
Q9R194
Residue number A
51
Residue number B
196
Peptide name
Cryptochrome-2
Ligandability
Cysteine 51 of Cryptochrome-2
Cysteine 196 of Cryptochrome-2
4i6g A 381 A 420
A redox-regulated disulphide may form within Cryptochrome-2 between cysteines 381 and 420. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
4i6g
Structure name
a vertebrate cryptochrome with fad
Structure deposition date
2012-11-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
100
Peptide accession
Q9R194
Residue number A
381
Residue number B
420
Peptide name
Cryptochrome-2
Ligandability
Cysteine 381 of Cryptochrome-2
Cysteine 420 of Cryptochrome-2
4i6j A 48 A 51
A redox-regulated disulphide may form within Cryptochrome-2 between cysteines 48 and 51. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
4i6j
Structure name
a ubiquitin ligase-substrate complex
Structure deposition date
2012-11-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
75
Peptide accession
Q9R194
Residue number A
48
Residue number B
51
Peptide name
Cryptochrome-2
Ligandability
Cysteine 48 of Cryptochrome-2
Cysteine 51 of Cryptochrome-2
4i6g A 381 A 432
A redox-regulated disulphide may form within Cryptochrome-2 between cysteines 381 and 432. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
4i6g
Structure name
a vertebrate cryptochrome with fad
Structure deposition date
2012-11-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
8
% buried
100
Peptide accession
Q9R194
Residue number A
381
Residue number B
432
Peptide name
Cryptochrome-2
Ligandability
Cysteine 381 of Cryptochrome-2
Cysteine 432 of Cryptochrome-2
4i6g A 420 A 430
A redox-regulated disulphide may form within Cryptochrome-2 between cysteines 420 and 430. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
4i6g
Structure name
a vertebrate cryptochrome with fad
Structure deposition date
2012-11-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
11
% buried
100
Peptide accession
Q9R194
Residue number A
420
Residue number B
430
Peptide name
Cryptochrome-2
Ligandability
Cysteine 420 of Cryptochrome-2
Cysteine 430 of Cryptochrome-2
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