nitric-oxide synthase (NADPH)
Intermolecular
Cysteine 94 and cysteine 94
Cysteine 99 and cysteine 99
Cysteine 382 and cysteine 382
Intramolecular
Cysteine 94 and cysteine 99
Cysteine 184 and cysteine 441
6nh2 C 94 D 94
A redox-regulated disulphide may form between two units of nitric-oxide synthase (NADPH) at cysteines 94 and 94.
Details
Redox score ?
74
PDB code
6nh2
Structure name
structure of human endothelial nitric oxide synthase heme domain in complex with (r)-6-(3-fluoro-5-(2-(pyrrolidin-2-yl)ethyl)phenethyl)- 4-methylpyridin-2-amine
Structure deposition date
2018-12-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide A name
nitric-oxide synthase (NADPH)
Peptide B name
nitric-oxide synthase (NADPH)
Peptide A accession
A0S0A6
Peptide B accession
A0S0A6
Peptide A residue number
94
Peptide B residue number
94
Ligandability
6nh1 A 99 B 99
A redox-regulated disulphide may form between two units of nitric-oxide synthase (NADPH) at cysteines 99 and 99.
Details
Redox score ?
69
PDB code
6nh1
Structure name
structure of human endothelial nitric oxide synthase heme domain in complex with 6-(3-fluoro-5-(3-(methylamino)prop-1-yn-1-yl)phenethyl)- 4-methylpyridin-2-amine
Structure deposition date
2018-12-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide A name
nitric-oxide synthase (NADPH)
Peptide B name
nitric-oxide synthase (NADPH)
Peptide A accession
A0S0A6
Peptide B accession
A0S0A6
Peptide A residue number
99
Peptide B residue number
99
Ligandability
6nh2 B 382 C 382
A redox-regulated disulphide may form between two units of nitric-oxide synthase (NADPH) at cysteines 382 and 382. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
6nh2
Structure name
structure of human endothelial nitric oxide synthase heme domain in complex with (r)-6-(3-fluoro-5-(2-(pyrrolidin-2-yl)ethyl)phenethyl)- 4-methylpyridin-2-amine
Structure deposition date
2018-12-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide A name
nitric-oxide synthase (NADPH)
Peptide B name
nitric-oxide synthase (NADPH)
Peptide A accession
A0S0A6
Peptide B accession
A0S0A6
Peptide A residue number
382
Peptide B residue number
382
Ligandability
6nh1 A 94 A 99
A redox-regulated disulphide may form within nitric-oxide synthase (NADPH) between cysteines 94 and 99.
Details
Redox score ?
74
PDB code
6nh1
Structure name
structure of human endothelial nitric oxide synthase heme domain in complex with 6-(3-fluoro-5-(3-(methylamino)prop-1-yn-1-yl)phenethyl)- 4-methylpyridin-2-amine
Structure deposition date
2018-12-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
A0S0A6
Residue number A
94
Residue number B
99
Peptide name
nitric-oxide synthase (NADPH)
Ligandability
Cysteine 94 of nitric-oxide synthase (NADPH)
Cysteine 99 of nitric-oxide synthase (NADPH)
6nh4 A 184 A 441
A redox-regulated disulphide may form within nitric-oxide synthase (NADPH) between cysteines 184 and 441. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6nh4
Structure name
structure of human endothelial nitric oxide synthase heme domain in complex with 6-(3-fluoro-5-(2-((2r,4s)-4-fluoropyrrolidin-2-yl) ethyl)phenethyl)-4-methylpyridin-2-amine
Structure deposition date
2018-12-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
A0S0A6
Residue number A
184
Residue number B
441
Peptide name
nitric-oxide synthase (NADPH)
Ligandability
Cysteine 184 of nitric-oxide synthase (NADPH)
Cysteine 441 of nitric-oxide synthase (NADPH)
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