Prostaglandin G/H synthase 2
Intramolecular
Cysteine 22 and cysteine 145
Cysteine 44 and cysteine 54
Cysteine 26 and cysteine 42
Cysteine 555 and cysteine 561
Cysteine 21 and cysteine 32
Cysteine 26 and cysteine 32
Cysteine 42 and cysteine 54
Cysteine 26 and cysteine 54
Cysteine 32 and cysteine 42
Cysteine 42 and cysteine 44
More...Cysteine 21 and cysteine 26
Cysteine 26 and cysteine 44
Cysteine 21 and cysteine 42
Cysteine 21 and cysteine 22
Cysteine 22 and cysteine 32
Cysteine 21 and cysteine 145
Cysteine 32 and cysteine 54
Cysteine 32 and cysteine 145
5f19 B 37 B 159
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 22 and 145 (37 and 159 respectively in this structure).
Details
Redox score ?
87
PDB code
5f19
Structure name
the crystal structure of aspirin acetylated human cyclooxygenase-2
Structure deposition date
2015-11-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
22
Residue number B
145
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 22 of Prostaglandin G/H synthase 2
Cysteine 145 of Prostaglandin G/H synthase 2
5f1a A 59 A 69
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 44 and 54 (59 and 69 respectively in this structure).
Details
Redox score ?
87
PDB code
5f1a
Structure name
the crystal structure of salicylate bound to human cyclooxygenase-2
Structure deposition date
2015-11-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
44
Residue number B
54
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 44 of Prostaglandin G/H synthase 2
Cysteine 54 of Prostaglandin G/H synthase 2
5kir A 41 A 57
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 26 and 42 (41 and 57 respectively in this structure).
Details
Redox score ?
85
PDB code
5kir
Structure name
the structure of vioxx bound to human cox-2
Structure deposition date
2016-06-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
26
Residue number B
42
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 26 of Prostaglandin G/H synthase 2
Cysteine 42 of Prostaglandin G/H synthase 2
5ikt B 569 B 575
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 555 and 561 (569 and 575 respectively in this structure).
Details
Redox score ?
85
PDB code
5ikt
Structure name
the structure of tolfenamic acid bound to human cyclooxygenase-2
Structure deposition date
2016-03-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
555
Residue number B
561
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 555 of Prostaglandin G/H synthase 2
Cysteine 561 of Prostaglandin G/H synthase 2
5ikr B 36 B 47
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 21 and 32 (36 and 47 respectively in this structure).
Details
Redox score ?
81
PDB code
5ikr
Structure name
the structure of mefenamic acid bound to human cyclooxygenase-2
Structure deposition date
2016-03-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
21
Residue number B
32
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 21 of Prostaglandin G/H synthase 2
Cysteine 32 of Prostaglandin G/H synthase 2
5kir A 41 A 47
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 26 and 32 (41 and 47 respectively in this structure).
Details
Redox score ?
72
PDB code
5kir
Structure name
the structure of vioxx bound to human cox-2
Structure deposition date
2016-06-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
26
Residue number B
32
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 26 of Prostaglandin G/H synthase 2
Cysteine 32 of Prostaglandin G/H synthase 2
5ikv B 57 B 69
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 42 and 54 (57 and 69 respectively in this structure).
Details
Redox score ?
69
PDB code
5ikv
Structure name
the structure of flufenamic acid bound to human cyclooxygenase-2
Structure deposition date
2016-03-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
42
Residue number B
54
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 42 of Prostaglandin G/H synthase 2
Cysteine 54 of Prostaglandin G/H synthase 2
5f19 B 41 B 69
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 26 and 54 (41 and 69 respectively in this structure).
Details
Redox score ?
69
PDB code
5f19
Structure name
the crystal structure of aspirin acetylated human cyclooxygenase-2
Structure deposition date
2015-11-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
26
Residue number B
54
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 26 of Prostaglandin G/H synthase 2
Cysteine 54 of Prostaglandin G/H synthase 2
5ikt B 47 B 57
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 32 and 42 (47 and 57 respectively in this structure).
Details
Redox score ?
65
PDB code
5ikt
Structure name
the structure of tolfenamic acid bound to human cyclooxygenase-2
Structure deposition date
2016-03-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
32
Residue number B
42
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 32 of Prostaglandin G/H synthase 2
Cysteine 42 of Prostaglandin G/H synthase 2
3nt1 B 57 B 59
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 42 and 44 (57 and 59 respectively in this structure).
Details
Redox score ?
63
PDB code
3nt1
Structure name
high resolution structure of naproxen:cox-2 complex
Structure deposition date
2010-07-02
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q543K3
Residue number A
42
Residue number B
44
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 42 of Prostaglandin G/H synthase 2
Cysteine 44 of Prostaglandin G/H synthase 2
5ikq B 36 B 41
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 21 and 26 (36 and 41 respectively in this structure).
Details
Redox score ?
61
PDB code
5ikq
Structure name
the structure of meclofenamic acid bound to human cyclooxygenase-2
Structure deposition date
2016-03-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
21
Residue number B
26
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 21 of Prostaglandin G/H synthase 2
Cysteine 26 of Prostaglandin G/H synthase 2
5ikv B 41 B 59
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 26 and 44 (41 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
5ikv
Structure name
the structure of flufenamic acid bound to human cyclooxygenase-2
Structure deposition date
2016-03-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
26
Residue number B
44
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 26 of Prostaglandin G/H synthase 2
Cysteine 44 of Prostaglandin G/H synthase 2
5kir B 36 B 57
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 21 and 42 (36 and 57 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5kir
Structure name
the structure of vioxx bound to human cox-2
Structure deposition date
2016-06-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
21
Residue number B
42
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 21 of Prostaglandin G/H synthase 2
Cysteine 42 of Prostaglandin G/H synthase 2
4rrz D 36 D 37
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 21 and 22 (36 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
4rrz
Structure name
crystal structure of apo murine h90w cyclooxygenase-2 complexed with lumiracoxib
Structure deposition date
2014-11-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q05769
Residue number A
21
Residue number B
22
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 21 of Prostaglandin G/H synthase 2
Cysteine 22 of Prostaglandin G/H synthase 2
5kir B 37 B 47
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 22 and 32 (37 and 47 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
5kir
Structure name
the structure of vioxx bound to human cox-2
Structure deposition date
2016-06-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
22
Residue number B
32
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 22 of Prostaglandin G/H synthase 2
Cysteine 32 of Prostaglandin G/H synthase 2
5f19 B 36 B 159
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 21 and 145 (36 and 159 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
5f19
Structure name
the crystal structure of aspirin acetylated human cyclooxygenase-2
Structure deposition date
2015-11-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
21
Residue number B
145
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 21 of Prostaglandin G/H synthase 2
Cysteine 145 of Prostaglandin G/H synthase 2
5f1a B 47 B 69
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 32 and 54 (47 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5f1a
Structure name
the crystal structure of salicylate bound to human cyclooxygenase-2
Structure deposition date
2015-11-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
32
Residue number B
54
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 32 of Prostaglandin G/H synthase 2
Cysteine 54 of Prostaglandin G/H synthase 2
5ikv A 47 A 159
A redox-regulated disulphide may form within Prostaglandin G/H synthase 2 between cysteines 32 and 145 (47 and 159 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5ikv
Structure name
the structure of flufenamic acid bound to human cyclooxygenase-2
Structure deposition date
2016-03-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35354
Residue number A
32
Residue number B
145
Peptide name
Prostaglandin G/H synthase 2
Ligandability
Cysteine 32 of Prostaglandin G/H synthase 2
Cysteine 145 of Prostaglandin G/H synthase 2
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