26S proteasome non-ATPase regulatory subunit 2
Intermolecular
Cysteine 236 and cysteine 58 of 26S proteasome regulatory subunit 4 L
Intramolecular
Cysteine 205 and cysteine 236 L
Cysteine 205 and cysteine 251
Cysteine 205 and cysteine 230 L
Cysteine 230 and cysteine 251 L
Cysteine 251 and cysteine 285
Cysteine 448 and cysteine 459 L
Cysteine 598 and cysteine 779
Cysteine 522 and cysteine 779
6epc Z 236 I 58
A redox-regulated disulphide may form between cysteine 236 of 26S proteasome non-ATPase regulatory subunit 2 and cysteine 58 of 26S proteasome regulatory subunit 4. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
6epc
Structure name
ground state 26s proteasome (gs2)
Structure deposition date
2017-10-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
80
Peptide A name
26S proteasome non-ATPase regulatory subunit 2
Peptide B name
26S proteasome regulatory subunit 4
Peptide A accession
Q4FZT9
Peptide B accession
P62193
Peptide A residue number
236
Peptide B residue number
58
Ligandability
Cysteine 236 of 26S proteasome non-ATPase regulatory subunit 2
Cysteine 58 of 26S proteasome regulatory subunit 4
5ln3 Z 205 Z 236
A redox-regulated disulphide may form within 26S proteasome non-ATPase regulatory subunit 2 between cysteines 205 and 236.
Details
Redox score ?
74
PDB code
5ln3
Structure name
the human 26s proteasome at 6
Structure deposition date
2016-08-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
22
Peptide accession
Q13200
Residue number A
205
Residue number B
236
Peptide name
26S proteasome non-ATPase regulatory subunit 2
Ligandability
Cysteine 205 of 26S proteasome non-ATPase regulatory subunit 2
Cysteine 236 of 26S proteasome non-ATPase regulatory subunit 2
5l4k Z 205 Z 251
A redox-regulated disulphide may form within 26S proteasome non-ATPase regulatory subunit 2 between cysteines 205 and 251.
Details
Redox score ?
69
PDB code
5l4k
Structure name
the human 26s proteasome lid
Structure deposition date
2016-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
48
Peptide accession
Q13200
Residue number A
205
Residue number B
251
Peptide name
26S proteasome non-ATPase regulatory subunit 2
Ligandability
Cysteine 205 of 26S proteasome non-ATPase regulatory subunit 2
Cysteine 251 of 26S proteasome non-ATPase regulatory subunit 2
5t0h f 46 f 71
A redox-regulated disulphide may form within 26S proteasome non-ATPase regulatory subunit 2 between cysteines 205 and 230 (46 and 71 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5t0h
Structure name
structural basis for dynamic regulation of the human 26s proteasome
Structure deposition date
2016-08-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
32
Peptide accession
Q13200
Residue number A
205
Residue number B
230
Peptide name
26S proteasome non-ATPase regulatory subunit 2
Ligandability
Cysteine 205 of 26S proteasome non-ATPase regulatory subunit 2
Cysteine 230 of 26S proteasome non-ATPase regulatory subunit 2
5ln3 Z 230 Z 251
A redox-regulated disulphide may form within 26S proteasome non-ATPase regulatory subunit 2 between cysteines 230 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5ln3
Structure name
the human 26s proteasome at 6
Structure deposition date
2016-08-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
46
Peptide accession
Q13200
Residue number A
230
Residue number B
251
Peptide name
26S proteasome non-ATPase regulatory subunit 2
Ligandability
Cysteine 230 of 26S proteasome non-ATPase regulatory subunit 2
Cysteine 251 of 26S proteasome non-ATPase regulatory subunit 2
5t0j f 92 f 126
A redox-regulated disulphide may form within 26S proteasome non-ATPase regulatory subunit 2 between cysteines 251 and 285 (92 and 126 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5t0j
Structure name
structural basis for dynamic regulation of the human 26s proteasome
Structure deposition date
2016-08-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
61
Peptide accession
Q13200
Residue number A
251
Residue number B
285
Peptide name
26S proteasome non-ATPase regulatory subunit 2
Ligandability
Cysteine 251 of 26S proteasome non-ATPase regulatory subunit 2
Cysteine 285 of 26S proteasome non-ATPase regulatory subunit 2
5vhn f 448 f 459
A redox-regulated disulphide may form within 26S proteasome non-ATPase regulatory subunit 2 between cysteines 448 and 459. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
5vhn
Structure name
conformational landscape of the p28-bound human proteasome regulatory particle
Structure deposition date
2017-04-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
62
Peptide accession
Q13200
Residue number A
448
Residue number B
459
Peptide name
26S proteasome non-ATPase regulatory subunit 2
Ligandability
Cysteine 448 of 26S proteasome non-ATPase regulatory subunit 2
Cysteine 459 of 26S proteasome non-ATPase regulatory subunit 2
5vhi f 598 f 779
A redox-regulated disulphide may form within 26S proteasome non-ATPase regulatory subunit 2 between cysteines 598 and 779. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
5vhi
Structure name
conformational landscape of the p28-bound human proteasome regulatory particle
Structure deposition date
2017-04-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
97
Peptide accession
Q13200
Residue number A
598
Residue number B
779
Peptide name
26S proteasome non-ATPase regulatory subunit 2
Ligandability
Cysteine 598 of 26S proteasome non-ATPase regulatory subunit 2
Cysteine 779 of 26S proteasome non-ATPase regulatory subunit 2
5vhi f 522 f 779
A redox-regulated disulphide may form within 26S proteasome non-ATPase regulatory subunit 2 between cysteines 522 and 779. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
5vhi
Structure name
conformational landscape of the p28-bound human proteasome regulatory particle
Structure deposition date
2017-04-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
11
% buried
97
Peptide accession
Q13200
Residue number A
522
Residue number B
779
Peptide name
26S proteasome non-ATPase regulatory subunit 2
Ligandability
Cysteine 522 of 26S proteasome non-ATPase regulatory subunit 2
Cysteine 779 of 26S proteasome non-ATPase regulatory subunit 2
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