THO complex subunit 3
Intermolecular
Cysteine 503 of THO complex subunit 2 and cysteine 258
Cysteine 503 of THO complex subunit 2 and cysteine 261
Cysteine 500 of THO complex subunit 2 and cysteine 261
Cysteine 500 of THO complex subunit 2 and cysteine 258
Intramolecular
Cysteine 306 and cysteine 326
Cysteine 227 and cysteine 229
Cysteine 106 and cysteine 148
Cysteine 258 and cysteine 261
7apk j 503 k 258
A redox-regulated disulphide may form between cysteine 503 of THO complex subunit 2 and cysteine 258 of THO complex subunit 3.
Details
Redox score ?
79
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
4
% buried
100
Peptide A name
THO complex subunit 2
Peptide B name
THO complex subunit 3
Peptide A accession
Q8NI27
Peptide B accession
Q96J01
Peptide A residue number
503
Peptide B residue number
258
Ligandability
Cysteine 503 of THO complex subunit 2
Cysteine 258 of THO complex subunit 3
7apk J 503 K 261
A redox-regulated disulphide may form between cysteine 503 of THO complex subunit 2 and cysteine 261 of THO complex subunit 3. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
4
% buried
100
Peptide A name
THO complex subunit 2
Peptide B name
THO complex subunit 3
Peptide A accession
Q8NI27
Peptide B accession
Q96J01
Peptide A residue number
503
Peptide B residue number
261
Ligandability
Cysteine 503 of THO complex subunit 2
Cysteine 261 of THO complex subunit 3
7apk b 500 c 261
A redox-regulated disulphide may form between cysteine 500 of THO complex subunit 2 and cysteine 261 of THO complex subunit 3. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
100
Peptide A name
THO complex subunit 2
Peptide B name
THO complex subunit 3
Peptide A accession
Q8NI27
Peptide B accession
Q96J01
Peptide A residue number
500
Peptide B residue number
261
Ligandability
Cysteine 500 of THO complex subunit 2
Cysteine 261 of THO complex subunit 3
7apk J 500 K 258
A redox-regulated disulphide may form between cysteine 500 of THO complex subunit 2 and cysteine 258 of THO complex subunit 3. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
19
% buried
100
Peptide A name
THO complex subunit 2
Peptide B name
THO complex subunit 3
Peptide A accession
Q8NI27
Peptide B accession
Q96J01
Peptide A residue number
500
Peptide B residue number
258
Ligandability
Cysteine 500 of THO complex subunit 2
Cysteine 258 of THO complex subunit 3
7apk c 306 c 326
A redox-regulated disulphide may form within THO complex subunit 3 between cysteines 306 and 326.
Details
Redox score ?
69
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
42
Peptide accession
Q96J01
Residue number A
306
Residue number B
326
Peptide name
THO complex subunit 3
Ligandability
Cysteine 306 of THO complex subunit 3
Cysteine 326 of THO complex subunit 3
7apk C 227 C 229
A redox-regulated disulphide may form within THO complex subunit 3 between cysteines 227 and 229. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
100
Peptide accession
Q96J01
Residue number A
227
Residue number B
229
Peptide name
THO complex subunit 3
Ligandability
Cysteine 227 of THO complex subunit 3
Cysteine 229 of THO complex subunit 3
7apk K 106 K 148
A redox-regulated disulphide may form within THO complex subunit 3 between cysteines 106 and 148. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
Q96J01
Residue number A
106
Residue number B
148
Peptide name
THO complex subunit 3
Ligandability
Cysteine 106 of THO complex subunit 3
Cysteine 148 of THO complex subunit 3
7apk K 258 K 261
A redox-regulated disulphide may form within THO complex subunit 3 between cysteines 258 and 261. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
7apk
Structure name
structure of the human tho - uap56 complex
Structure deposition date
2020-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
100
Peptide accession
Q96J01
Residue number A
258
Residue number B
261
Peptide name
THO complex subunit 3
Ligandability
Cysteine 258 of THO complex subunit 3
Cysteine 261 of THO complex subunit 3
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