Kelch-like ECH-associated protein 1
Intermolecular
Cysteine 434 and cysteine 434
Cysteine 489 and cysteine 434
Cysteine 434 and cysteine 395 L
Cysteine 434 and cysteine 406 L
Cysteine 518 and cysteine 489
Intramolecular
Cysteine 395 and cysteine 406 L
Cysteine 151 and cysteine 171 L
Cysteine 368 and cysteine 395 L
Cysteine 368 and cysteine 406 L
Cysteine 513 and cysteine 518
6sp4 E 434 F 434
A redox-regulated disulphide may form between two units of Kelch-like ECH-associated protein 1 at cysteines 434 and 434.
Details
Redox score ?
84
PDB code
6sp4
Structure name
keap1 in complex with compound 23
Structure deposition date
2019-08-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
Kelch-like ECH-associated protein 1
Peptide B name
Kelch-like ECH-associated protein 1
Peptide A accession
Q14145
Peptide B accession
Q14145
Peptide A residue number
434
Peptide B residue number
434
Ligandability
5x54 A 489 B 434
A redox-regulated disulphide may form between two units of Kelch-like ECH-associated protein 1 at cysteines 489 and 434.
Details
Redox score ?
69
PDB code
5x54
Structure name
crystal structure of the keap1 kelch domain in complex with a tetrapeptide
Structure deposition date
2017-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
96
Peptide A name
Kelch-like ECH-associated protein 1
Peptide B name
Kelch-like ECH-associated protein 1
Peptide A accession
Q14145
Peptide B accession
Q14145
Peptide A residue number
489
Peptide B residue number
434
Ligandability
Cysteine 489 of Kelch-like ECH-associated protein 1
Cysteine 434 of Kelch-like ECH-associated protein 1
6uf0 A 434 B 395
A redox-regulated disulphide may form between two units of Kelch-like ECH-associated protein 1 at cysteines 434 and 395. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
6uf0
Structure name
crystal structure of n-(4-((4-methoxy-n-(2,2,2-trifluoroethyl)phenyl) sulfonamido)isoquinolin-1-yl)-n-((4-methoxyphenyl)sulfonyl)glycine bound to human keap1 kelch domain
Structure deposition date
2019-09-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
58
Peptide A name
Kelch-like ECH-associated protein 1
Peptide B name
Kelch-like ECH-associated protein 1
Peptide A accession
Q14145
Peptide B accession
Q14145
Peptide A residue number
434
Peptide B residue number
395
Ligandability
Cysteine 434 of Kelch-like ECH-associated protein 1
Cysteine 395 of Kelch-like ECH-associated protein 1
6uf0 A 434 B 406
A redox-regulated disulphide may form between two units of Kelch-like ECH-associated protein 1 at cysteines 434 and 406. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6uf0
Structure name
crystal structure of n-(4-((4-methoxy-n-(2,2,2-trifluoroethyl)phenyl) sulfonamido)isoquinolin-1-yl)-n-((4-methoxyphenyl)sulfonyl)glycine bound to human keap1 kelch domain
Structure deposition date
2019-09-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
53
Peptide A name
Kelch-like ECH-associated protein 1
Peptide B name
Kelch-like ECH-associated protein 1
Peptide A accession
Q14145
Peptide B accession
Q14145
Peptide A residue number
434
Peptide B residue number
406
Ligandability
Cysteine 434 of Kelch-like ECH-associated protein 1
Cysteine 406 of Kelch-like ECH-associated protein 1
5wg1 A 518 B 489
A redox-regulated disulphide may form between two units of Kelch-like ECH-associated protein 1 at cysteines 518 and 489. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
5wg1
Structure name
kelch domain of human keap1 bound to mutant nrf2 eage peptide
Structure deposition date
2017-07-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
95
Peptide A name
Kelch-like ECH-associated protein 1
Peptide B name
Kelch-like ECH-associated protein 1
Peptide A accession
Q14145
Peptide B accession
Q14145
Peptide A residue number
518
Peptide B residue number
489
Ligandability
Cysteine 518 of Kelch-like ECH-associated protein 1
Cysteine 489 of Kelch-like ECH-associated protein 1
7k2r A 395 A 406
A redox-regulated disulphide may form within Kelch-like ECH-associated protein 1 between cysteines 395 and 406.
Details
Redox score ?
81
PDB code
7k2r
Structure name
kelch domain of human keap1 bound to nrf2-based cyclic peptide, c[lha- deetge]
Structure deposition date
2020-09-08
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
34
Peptide accession
Q14145
Residue number A
395
Residue number B
406
Peptide name
Kelch-like ECH-associated protein 1
Ligandability
Cysteine 395 of Kelch-like ECH-associated protein 1
Cysteine 406 of Kelch-like ECH-associated protein 1
5nlb A 151 A 171
A redox-regulated disulphide may form within Kelch-like ECH-associated protein 1 between cysteines 151 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5nlb
Structure name
crystal structure of human cul3 n-terminal domain bound to keap1 btb and 3-box
Structure deposition date
2017-04-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
18
Peptide accession
Q14145
Residue number A
151
Residue number B
171
Peptide name
Kelch-like ECH-associated protein 1
Ligandability
Cysteine 151 of Kelch-like ECH-associated protein 1
Cysteine 171 of Kelch-like ECH-associated protein 1
7k2m A 368 A 395
A redox-regulated disulphide may form within Kelch-like ECH-associated protein 1 between cysteines 368 and 395. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7k2m
Structure name
kelch domain of human keap1 bound to nrf2 cyclic peptide, c[gepetge]
Structure deposition date
2020-09-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
72
Peptide accession
Q14145
Residue number A
368
Residue number B
395
Peptide name
Kelch-like ECH-associated protein 1
Ligandability
Cysteine 368 of Kelch-like ECH-associated protein 1
Cysteine 395 of Kelch-like ECH-associated protein 1
7k2g A 368 A 406
A redox-regulated disulphide may form within Kelch-like ECH-associated protein 1 between cysteines 368 and 406. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
7k2g
Structure name
kelch domain of human keap1 bound to nrf2 cyclic peptide, c[gdeeage]
Structure deposition date
2020-09-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
76
Peptide accession
Q14145
Residue number A
368
Residue number B
406
Peptide name
Kelch-like ECH-associated protein 1
Ligandability
Cysteine 368 of Kelch-like ECH-associated protein 1
Cysteine 406 of Kelch-like ECH-associated protein 1
7k2h B 513 B 518
A redox-regulated disulphide may form within Kelch-like ECH-associated protein 1 between cysteines 513 and 518. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
7k2h
Structure name
kelch domain of human keap1 bound to nrf2 cyclic peptide, c[gdpetge]
Structure deposition date
2020-09-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
97
Peptide accession
Q14145
Residue number A
513
Residue number B
518
Peptide name
Kelch-like ECH-associated protein 1
Ligandability
Cysteine 513 of Kelch-like ECH-associated protein 1
Cysteine 518 of Kelch-like ECH-associated protein 1
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