RCC1-like G exchanging factor-like protein
Intramolecular
Cysteine 294 and cysteine 343
Cysteine 294 and cysteine 348
Cysteine 294 and cysteine 295
Cysteine 343 and cysteine 348
Cysteine 181 and cysteine 237
Cysteine 343 and cysteine 401
Cysteine 295 and cysteine 343
Cysteine 114 and cysteine 451
Cysteine 401 and cysteine 451
Cysteine 348 and cysteine 401
More...Cysteine 114 and cysteine 181
Cysteine 206 and cysteine 254
Cysteine 425 and cysteine 451
Cysteine 206 and cysteine 237
Cysteine 237 and cysteine 254
Cysteine 114 and cysteine 425
Cysteine 295 and cysteine 348
5xgs B 294 B 343
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 294 and 343.
Details
Redox score ?
71
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
104
Minimum pKa ?
5
% buried
100
Peptide accession
Q96I51
Residue number A
294
Residue number B
343
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 294 of RCC1-like G exchanging factor-like protein
Cysteine 343 of RCC1-like G exchanging factor-like protein
5xgs B 294 B 348
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 294 and 348.
Details
Redox score ?
63
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
109
Minimum pKa ?
5
% buried
100
Peptide accession
Q96I51
Residue number A
294
Residue number B
348
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 294 of RCC1-like G exchanging factor-like protein
Cysteine 348 of RCC1-like G exchanging factor-like protein
5xgs B 294 B 295
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 294 and 295. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
106
Minimum pKa ?
5
% buried
100
Peptide accession
Q96I51
Residue number A
294
Residue number B
295
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 294 of RCC1-like G exchanging factor-like protein
Cysteine 295 of RCC1-like G exchanging factor-like protein
5xgs B 343 B 348
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 343 and 348. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
108
Minimum pKa ?
15
% buried
100
Peptide accession
Q96I51
Residue number A
343
Residue number B
348
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 343 of RCC1-like G exchanging factor-like protein
Cysteine 348 of RCC1-like G exchanging factor-like protein
5xgs A 181 A 237
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 181 and 237. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
106
Minimum pKa ?
12
% buried
100
Peptide accession
Q96I51
Residue number A
181
Residue number B
237
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 181 of RCC1-like G exchanging factor-like protein
Cysteine 237 of RCC1-like G exchanging factor-like protein
5xgs A 343 A 401
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 343 and 401. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
99
Minimum pKa ?
13
% buried
100
Peptide accession
Q96I51
Residue number A
343
Residue number B
401
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 343 of RCC1-like G exchanging factor-like protein
Cysteine 401 of RCC1-like G exchanging factor-like protein
5xgs A 295 A 343
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 295 and 343. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
103
Minimum pKa ?
13
% buried
100
Peptide accession
Q96I51
Residue number A
295
Residue number B
343
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 295 of RCC1-like G exchanging factor-like protein
Cysteine 343 of RCC1-like G exchanging factor-like protein
5xgs B 114 B 451
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 114 and 451. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
105
Minimum pKa ?
13
% buried
100
Peptide accession
Q96I51
Residue number A
114
Residue number B
451
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 114 of RCC1-like G exchanging factor-like protein
Cysteine 451 of RCC1-like G exchanging factor-like protein
5xgs A 401 A 451
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 401 and 451. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
99
Minimum pKa ?
13
% buried
100
Peptide accession
Q96I51
Residue number A
401
Residue number B
451
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 401 of RCC1-like G exchanging factor-like protein
Cysteine 451 of RCC1-like G exchanging factor-like protein
5xgs B 348 B 401
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 348 and 401. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
105
Minimum pKa ?
13
% buried
100
Peptide accession
Q96I51
Residue number A
348
Residue number B
401
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 348 of RCC1-like G exchanging factor-like protein
Cysteine 401 of RCC1-like G exchanging factor-like protein
5xgs B 114 B 181
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 114 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
107
Minimum pKa ?
12
% buried
100
Peptide accession
Q96I51
Residue number A
114
Residue number B
181
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 114 of RCC1-like G exchanging factor-like protein
Cysteine 181 of RCC1-like G exchanging factor-like protein
5xgs B 206 B 254
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 206 and 254. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
100
Peptide accession
Q96I51
Residue number A
206
Residue number B
254
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 206 of RCC1-like G exchanging factor-like protein
Cysteine 254 of RCC1-like G exchanging factor-like protein
5xgs A 425 A 451
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 425 and 451. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
100
Minimum pKa ?
12
% buried
98
Peptide accession
Q96I51
Residue number A
425
Residue number B
451
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 425 of RCC1-like G exchanging factor-like protein
Cysteine 451 of RCC1-like G exchanging factor-like protein
5xgs B 206 B 237
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 206 and 237. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
106
Minimum pKa ?
12
% buried
100
Peptide accession
Q96I51
Residue number A
206
Residue number B
237
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 206 of RCC1-like G exchanging factor-like protein
Cysteine 237 of RCC1-like G exchanging factor-like protein
5xgs A 237 A 254
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 237 and 254. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
97
Minimum pKa ?
13
% buried
100
Peptide accession
Q96I51
Residue number A
237
Residue number B
254
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 237 of RCC1-like G exchanging factor-like protein
Cysteine 254 of RCC1-like G exchanging factor-like protein
5xgs B 114 B 425
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 114 and 425. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
22
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
101
Minimum pKa ?
12
% buried
98
Peptide accession
Q96I51
Residue number A
114
Residue number B
425
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 114 of RCC1-like G exchanging factor-like protein
Cysteine 425 of RCC1-like G exchanging factor-like protein
5xgs A 295 A 348
A redox-regulated disulphide may form within RCC1-like G exchanging factor-like protein between cysteines 295 and 348. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
18
PDB code
5xgs
Structure name
crystal structure of human wbscr16
Structure deposition date
2017-04-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
108
Minimum pKa ?
13
% buried
100
Peptide accession
Q96I51
Residue number A
295
Residue number B
348
Peptide name
RCC1-like G exchanging factor-like protein
Ligandability
Cysteine 295 of RCC1-like G exchanging factor-like protein
Cysteine 348 of RCC1-like G exchanging factor-like protein
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