Nuclear receptor ROR-gamma
Intermolecular
Cysteine 393 and cysteine 393
Cysteine 455 and cysteine 455
Intramolecular
Cysteine 320 and cysteine 393
Cysteine 393 and cysteine 476
Cysteine 366 and cysteine 476
Cysteine 320 and cysteine 476
Cysteine 285 and cysteine 366
Cysteine 278 and cysteine 285
5w4v D 393 E 393
A redox-regulated disulphide may form between two units of Nuclear receptor ROR-gamma at cysteines 393 and 393.
Details
Redox score ?
82
PDB code
5w4v
Structure name
structure of rorgt bound to a tertiary alcohol
Structure deposition date
2017-06-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide A name
Nuclear receptor ROR-gamma
Peptide B name
Nuclear receptor ROR-gamma
Peptide A accession
P51449
Peptide B accession
P51449
Peptide A residue number
393
Peptide B residue number
393
Ligandability
5k3l B 455 D 455
A redox-regulated disulphide may form between two units of Nuclear receptor ROR-gamma at cysteines 455 and 455. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5k3l
Structure name
crystal structure of retinoic acid receptor-related orphan receptor (ror) gamma ligand binding domain complex with 444
Structure deposition date
2016-05-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
14
% buried
100
Peptide A name
Nuclear receptor ROR-gamma
Peptide B name
Nuclear receptor ROR-gamma
Peptide A accession
P51449
Peptide B accession
P51449
Peptide A residue number
455
Peptide B residue number
455
Ligandability
4nb6 A 299 A 372
A redox-regulated disulphide may form within Nuclear receptor ROR-gamma between cysteines 320 and 393 (299 and 372 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
4nb6
Structure name
crystal structure of the ligand binding domain of rorc with t0901317
Structure deposition date
2013-10-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
65
Peptide accession
P51449
Residue number A
320
Residue number B
393
Peptide name
Nuclear receptor ROR-gamma
Ligandability
Cysteine 320 of Nuclear receptor ROR-gamma
Cysteine 393 of Nuclear receptor ROR-gamma
5x8x A 393 A 476
A redox-regulated disulphide may form within Nuclear receptor ROR-gamma between cysteines 393 and 476. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
5x8x
Structure name
crystal structure of the mutant human ror gamma ligand binding domain with compound a
Structure deposition date
2017-03-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P51449
Residue number A
393
Residue number B
476
Peptide name
Nuclear receptor ROR-gamma
Ligandability
Cysteine 393 of Nuclear receptor ROR-gamma
Cysteine 476 of Nuclear receptor ROR-gamma
6a22 E 366 E 476
A redox-regulated disulphide may form within Nuclear receptor ROR-gamma between cysteines 366 and 476. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6a22
Structure name
ternary complex of human ror gamma ligand binding domain with compound t
Structure deposition date
2018-06-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
96
Peptide accession
P51449
Residue number A
366
Residue number B
476
Peptide name
Nuclear receptor ROR-gamma
Ligandability
Cysteine 366 of Nuclear receptor ROR-gamma
Cysteine 476 of Nuclear receptor ROR-gamma
5x8x A 320 A 476
A redox-regulated disulphide may form within Nuclear receptor ROR-gamma between cysteines 320 and 476. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5x8x
Structure name
crystal structure of the mutant human ror gamma ligand binding domain with compound a
Structure deposition date
2017-03-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P51449
Residue number A
320
Residue number B
476
Peptide name
Nuclear receptor ROR-gamma
Ligandability
Cysteine 320 of Nuclear receptor ROR-gamma
Cysteine 476 of Nuclear receptor ROR-gamma
7w3p A 285 A 366
A redox-regulated disulphide may form within Nuclear receptor ROR-gamma between cysteines 285 and 366. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
7w3p
Structure name
crystal structure of rorgamma in complex with natural inverse agonist
Structure deposition date
2021-11-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
87
Peptide accession
P51449
Residue number A
285
Residue number B
366
Peptide name
Nuclear receptor ROR-gamma
Ligandability
Cysteine 285 of Nuclear receptor ROR-gamma
Cysteine 366 of Nuclear receptor ROR-gamma
6ivx A 278 A 285
A redox-regulated disulphide may form within Nuclear receptor ROR-gamma between cysteines 278 and 285. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
6ivx
Structure name
discovery of the second generation ror gamma inhibitors composed of an azole scaffold
Structure deposition date
2018-12-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
84
Peptide accession
P51449
Residue number A
278
Residue number B
285
Peptide name
Nuclear receptor ROR-gamma
Ligandability
Cysteine 278 of Nuclear receptor ROR-gamma
Cysteine 285 of Nuclear receptor ROR-gamma
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