Condensin complex subunit 3
Intramolecular
Cysteine 564 and cysteine 607
Cysteine 317 and cysteine 343
Cysteine 560 and cysteine 564
Cysteine 607 and cysteine 610 L
Cysteine 843 and cysteine 883
Cysteine 340 and cysteine 343
Cysteine 610 and cysteine 611 L
Cysteine 607 and cysteine 611 L
Cysteine 564 and cysteine 611 L
6igx D 564 D 607
A redox-regulated disulphide may form within Condensin complex subunit 3 between cysteines 564 and 607. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
6igx
Structure name
crystal structure of human cap-g in complex with cap-h
Structure deposition date
2018-09-26
Thiol separation (Å)
5
Half-sphere exposure sum ?
96
Minimum pKa ?
13
% buried
100
Peptide accession
Q9BPX3
Residue number A
564
Residue number B
607
Peptide name
Condensin complex subunit 3
Ligandability
Cysteine 564 of Condensin complex subunit 3
Cysteine 607 of Condensin complex subunit 3
6igx B 317 B 343
A redox-regulated disulphide may form within Condensin complex subunit 3 between cysteines 317 and 343. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6igx
Structure name
crystal structure of human cap-g in complex with cap-h
Structure deposition date
2018-09-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
80
Peptide accession
Q9BPX3
Residue number A
317
Residue number B
343
Peptide name
Condensin complex subunit 3
Ligandability
Cysteine 317 of Condensin complex subunit 3
Cysteine 343 of Condensin complex subunit 3
6igx B 560 B 564
A redox-regulated disulphide may form within Condensin complex subunit 3 between cysteines 560 and 564. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6igx
Structure name
crystal structure of human cap-g in complex with cap-h
Structure deposition date
2018-09-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
11
% buried
89
Peptide accession
Q9BPX3
Residue number A
560
Residue number B
564
Peptide name
Condensin complex subunit 3
Ligandability
Cysteine 560 of Condensin complex subunit 3
Cysteine 564 of Condensin complex subunit 3
6igx D 607 D 610
A redox-regulated disulphide may form within Condensin complex subunit 3 between cysteines 607 and 610. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6igx
Structure name
crystal structure of human cap-g in complex with cap-h
Structure deposition date
2018-09-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
Q9BPX3
Residue number A
607
Residue number B
610
Peptide name
Condensin complex subunit 3
Ligandability
Cysteine 607 of Condensin complex subunit 3
Cysteine 610 of Condensin complex subunit 3
6igx B 843 B 883
A redox-regulated disulphide may form within Condensin complex subunit 3 between cysteines 843 and 883. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6igx
Structure name
crystal structure of human cap-g in complex with cap-h
Structure deposition date
2018-09-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
16
Peptide accession
Q9BPX3
Residue number A
843
Residue number B
883
Peptide name
Condensin complex subunit 3
Ligandability
Cysteine 843 of Condensin complex subunit 3
Cysteine 883 of Condensin complex subunit 3
6igx D 340 D 343
A redox-regulated disulphide may form within Condensin complex subunit 3 between cysteines 340 and 343. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6igx
Structure name
crystal structure of human cap-g in complex with cap-h
Structure deposition date
2018-09-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
88
Peptide accession
Q9BPX3
Residue number A
340
Residue number B
343
Peptide name
Condensin complex subunit 3
Ligandability
Cysteine 340 of Condensin complex subunit 3
Cysteine 343 of Condensin complex subunit 3
6igx D 610 D 611
A redox-regulated disulphide may form within Condensin complex subunit 3 between cysteines 610 and 611. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6igx
Structure name
crystal structure of human cap-g in complex with cap-h
Structure deposition date
2018-09-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
Q9BPX3
Residue number A
610
Residue number B
611
Peptide name
Condensin complex subunit 3
Ligandability
Cysteine 610 of Condensin complex subunit 3
Cysteine 611 of Condensin complex subunit 3
6igx D 607 D 611
A redox-regulated disulphide may form within Condensin complex subunit 3 between cysteines 607 and 611. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6igx
Structure name
crystal structure of human cap-g in complex with cap-h
Structure deposition date
2018-09-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
14
% buried
100
Peptide accession
Q9BPX3
Residue number A
607
Residue number B
611
Peptide name
Condensin complex subunit 3
Ligandability
Cysteine 607 of Condensin complex subunit 3
Cysteine 611 of Condensin complex subunit 3
6igx D 564 D 611
A redox-regulated disulphide may form within Condensin complex subunit 3 between cysteines 564 and 611. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
6igx
Structure name
crystal structure of human cap-g in complex with cap-h
Structure deposition date
2018-09-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
95
Minimum pKa ?
13
% buried
100
Peptide accession
Q9BPX3
Residue number A
564
Residue number B
611
Peptide name
Condensin complex subunit 3
Ligandability
Cysteine 564 of Condensin complex subunit 3
Cysteine 611 of Condensin complex subunit 3
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