Cytochrome P450 2C9
Intramolecular
Cysteine 175 and cysteine 179
Cysteine 172 and cysteine 175
Cysteine 164 and cysteine 486
Cysteine 151 and cysteine 172
Cysteine 338 and cysteine 151
Cysteine 338 and cysteine 179
Cysteine 172 and cysteine 179
1r9o A 175 A 179
A redox-regulated disulphide may form within Cytochrome P450 2C9 between cysteines 175 and 179.
Details
Redox score ?
63
PDB code
1r9o
Structure name
crystal structure of p4502c9 with flurbiprofen bound
Structure deposition date
2003-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
100
Peptide accession
P11712
Residue number A
175
Residue number B
179
Peptide name
Cytochrome P450 2C9
Ligandability
Cysteine 175 of Cytochrome P450 2C9
Cysteine 179 of Cytochrome P450 2C9
6vlt G 172 G 175
A redox-regulated disulphide may form within Cytochrome P450 2C9 between cysteines 172 and 175. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6vlt
Structure name
crystal structure of human p450 2c9*2 genetic variant in complex with losartan
Structure deposition date
2020-01-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
90
Peptide accession
P11712
Residue number A
172
Residue number B
175
Peptide name
Cytochrome P450 2C9
Ligandability
Cysteine 172 of Cytochrome P450 2C9
Cysteine 175 of Cytochrome P450 2C9
1og5 A 164 A 486
A redox-regulated disulphide may form within Cytochrome P450 2C9 between cysteines 164 and 486. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1og5
Structure name
structure of human cytochrome p450 cyp2c9
Structure deposition date
2003-04-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
26
Peptide accession
P11712
Residue number A
164
Residue number B
486
Peptide name
Cytochrome P450 2C9
Ligandability
Cysteine 164 of Cytochrome P450 2C9
Cysteine 486 of Cytochrome P450 2C9
6vlt F 151 F 172
A redox-regulated disulphide may form within Cytochrome P450 2C9 between cysteines 151 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6vlt
Structure name
crystal structure of human p450 2c9*2 genetic variant in complex with losartan
Structure deposition date
2020-01-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
59
Peptide accession
P11712
Residue number A
151
Residue number B
172
Peptide name
Cytochrome P450 2C9
Ligandability
Cysteine 151 of Cytochrome P450 2C9
Cysteine 172 of Cytochrome P450 2C9
6vlt G 144 G 151
A redox-regulated disulphide may form within Cytochrome P450 2C9 between cysteines 338 and 151 (144 and 151 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6vlt
Structure name
crystal structure of human p450 2c9*2 genetic variant in complex with losartan
Structure deposition date
2020-01-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
56
Peptide accession
P11712
Residue number A
338
Residue number B
151
Peptide name
Cytochrome P450 2C9
Ligandability
Cysteine 338 of Cytochrome P450 2C9
Cysteine 151 of Cytochrome P450 2C9
6vlt F 144 F 179
A redox-regulated disulphide may form within Cytochrome P450 2C9 between cysteines 338 and 179 (144 and 179 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6vlt
Structure name
crystal structure of human p450 2c9*2 genetic variant in complex with losartan
Structure deposition date
2020-01-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
81
Peptide accession
P11712
Residue number A
338
Residue number B
179
Peptide name
Cytochrome P450 2C9
Ligandability
Cysteine 338 of Cytochrome P450 2C9
Cysteine 179 of Cytochrome P450 2C9
6vlt H 172 H 179
A redox-regulated disulphide may form within Cytochrome P450 2C9 between cysteines 172 and 179. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6vlt
Structure name
crystal structure of human p450 2c9*2 genetic variant in complex with losartan
Structure deposition date
2020-01-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
14
% buried
90
Peptide accession
P11712
Residue number A
172
Residue number B
179
Peptide name
Cytochrome P450 2C9
Ligandability
Cysteine 172 of Cytochrome P450 2C9
Cysteine 179 of Cytochrome P450 2C9
If this tool was useful for finding a disulphide, please cite: