THO complex subunit 2
Intermolecular
Cysteine 503 and cysteine 258 of THO complex subunit 3
Cysteine 503 and cysteine 261 of THO complex subunit 3
Cysteine 500 and cysteine 261 of THO complex subunit 3
Cysteine 156 of THO complex subunit 1 and cysteine 202 L
Cysteine 500 and cysteine 258 of THO complex subunit 3
Intramolecular
Cysteine 500 and cysteine 503
Cysteine 436 and cysteine 482
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 A 156 B 202
A redox-regulated disulphide may form between cysteine 156 of THO complex subunit 1 and cysteine 202 of THO complex subunit 2. 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)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
53
Peptide A name
THO complex subunit 1
Peptide B name
THO complex subunit 2
Peptide A accession
Q96FV9
Peptide B accession
Q8NI27
Peptide A residue number
156
Peptide B residue number
202
Ligandability
Cysteine 156 of THO complex subunit 1
Cysteine 202 of THO complex subunit 2
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 b 500 b 503
A redox-regulated disulphide may form within THO complex subunit 2 between cysteines 500 and 503.
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 ?
86
Minimum pKa ?
4
% buried
100
Peptide accession
Q8NI27
Residue number A
500
Residue number B
503
Peptide name
THO complex subunit 2
Ligandability
Cysteine 500 of THO complex subunit 2
Cysteine 503 of THO complex subunit 2
7apk J 436 J 482
A redox-regulated disulphide may form within THO complex subunit 2 between cysteines 436 and 482. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
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 ?
51
Minimum pKa ?
9
% buried
16
Peptide accession
Q8NI27
Residue number A
436
Residue number B
482
Peptide name
THO complex subunit 2
Ligandability
Cysteine 436 of THO complex subunit 2
Cysteine 482 of THO complex subunit 2
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