Phospholipase A2, major isoenzyme
Intermolecular
Cysteine 99 and cysteine 99
Intramolecular
Cysteine 83 and cysteine 113
Cysteine 33 and cysteine 99
Cysteine 106 and cysteine 118
Cysteine 49 and cysteine 146
Cysteine 73 and cysteine 120
Cysteine 51 and cysteine 67
Cysteine 66 and cysteine 127
Cysteine 66 and cysteine 67
Cysteine 83 and cysteine 120
More...Cysteine 51 and cysteine 66
Cysteine 67 and cysteine 127
Cysteine 66 and cysteine 73
Cysteine 51 and cysteine 127
Cysteine 51 and cysteine 146
Cysteine 113 and cysteine 120
Cysteine 99 and cysteine 106
Cysteine 73 and cysteine 127
Cysteine 73 and cysteine 83
Cysteine 113 and cysteine 118
Cysteine 106 and cysteine 113
Cysteine 106 and cysteine 120
Cysteine 67 and cysteine 146
Cysteine 33 and cysteine 106
Cysteine 33 and cysteine 118
Cysteine 118 and cysteine 120
Cysteine 73 and cysteine 118
Cysteine 66 and cysteine 120
Cysteine 67 and cysteine 73
Cysteine 49 and cysteine 51
Cysteine 120 and cysteine 127
Cysteine 67 and cysteine 120
Cysteine 49 and cysteine 67
3fvi A 77 B 77
A redox-regulated disulphide may form between two units of Phospholipase A2, major isoenzyme at cysteines 99 and 99 (77 and 77 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
3fvi
Structure name
crystal structure of complex of phospholipase a2 with octyl sulfates
Structure deposition date
2009-01-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide A name
Phospholipase A2, major isoenzyme
Peptide B name
Phospholipase A2, major isoenzyme
Peptide A accession
P00592
Peptide B accession
P00592
Peptide A residue number
99
Peptide B residue number
99
Ligandability
3elo A 61 A 91
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 83 and 113 (61 and 91 respectively in this structure).
Details
Redox score ?
88
PDB code
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
83
Residue number B
113
Peptide name
Phospholipase A2
Ligandability
Cysteine 83 of Phospholipase A2
Cysteine 113 of Phospholipase A2
6q42 A 11 A 77
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 33 and 99 (11 and 77 respectively in this structure).
Details
Redox score ?
85
PDB code
6q42
Structure name
crystal structure of human pancreatic phospholipase a2
Structure deposition date
2018-12-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
33
Residue number B
99
Peptide name
Phospholipase A2
Ligandability
Cysteine 33 of Phospholipase A2
Cysteine 99 of Phospholipase A2
6q42 A 84 A 96
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 106 and 118 (84 and 96 respectively in this structure).
Details
Redox score ?
83
PDB code
6q42
Structure name
crystal structure of human pancreatic phospholipase a2
Structure deposition date
2018-12-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
106
Residue number B
118
Peptide name
Phospholipase A2
Ligandability
Cysteine 106 of Phospholipase A2
Cysteine 118 of Phospholipase A2
3elo A 27 A 124
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 49 and 146 (27 and 124 respectively in this structure).
Details
Redox score ?
83
PDB code
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
49
Residue number B
146
Peptide name
Phospholipase A2
Ligandability
Cysteine 49 of Phospholipase A2
Cysteine 146 of Phospholipase A2
3elo A 51 A 98
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 73 and 120 (51 and 98 respectively in this structure).
Details
Redox score ?
80
PDB code
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
73
Residue number B
120
Peptide name
Phospholipase A2
Ligandability
Cysteine 73 of Phospholipase A2
Cysteine 120 of Phospholipase A2
6q42 A 29 A 45
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 51 and 67 (29 and 45 respectively in this structure).
Details
Redox score ?
80
PDB code
6q42
Structure name
crystal structure of human pancreatic phospholipase a2
Structure deposition date
2018-12-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
51
Residue number B
67
Peptide name
Phospholipase A2
Ligandability
Cysteine 51 of Phospholipase A2
Cysteine 67 of Phospholipase A2
3elo A 44 A 105
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 66 and 127 (44 and 105 respectively in this structure).
Details
Redox score ?
79
PDB code
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
66
Residue number B
127
Peptide name
Phospholipase A2
Ligandability
Cysteine 66 of Phospholipase A2
Cysteine 127 of Phospholipase A2
6q42 B 44 B 45
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 66 and 67 (44 and 45 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6q42
Structure name
crystal structure of human pancreatic phospholipase a2
Structure deposition date
2018-12-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
66
Residue number B
67
Peptide name
Phospholipase A2
Ligandability
Cysteine 66 of Phospholipase A2
Cysteine 67 of Phospholipase A2
3elo A 61 A 98
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 83 and 120 (61 and 98 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
83
Residue number B
120
Peptide name
Phospholipase A2
Ligandability
Cysteine 83 of Phospholipase A2
Cysteine 120 of Phospholipase A2
6q42 B 29 B 44
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 51 and 66 (29 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
6q42
Structure name
crystal structure of human pancreatic phospholipase a2
Structure deposition date
2018-12-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
51
Residue number B
66
Peptide name
Phospholipase A2
Ligandability
Cysteine 51 of Phospholipase A2
Cysteine 66 of Phospholipase A2
3elo A 45 A 105
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 67 and 127 (45 and 105 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
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
67
Residue number B
127
Peptide name
Phospholipase A2
Ligandability
Cysteine 67 of Phospholipase A2
Cysteine 127 of Phospholipase A2
1sfw A 44 A 51
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 66 and 73 (44 and 51 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
1sfw
Structure name
porcine pancreas phospholipase a2, nmr, 18 structures
Structure deposition date
1996-02-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
66
Residue number B
73
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 66 of Phospholipase A2, major isoenzyme
Cysteine 73 of Phospholipase A2, major isoenzyme
1fx9 A 29 A 105
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 51 and 127 (29 and 105 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
1fx9
Structure name
carboxylic ester hydrolase complex (dimeric pla2 + mj33 inhibitor + sulphate ions)
Structure deposition date
2000-09-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
51
Residue number B
127
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 51 of Phospholipase A2, major isoenzyme
Cysteine 127 of Phospholipase A2, major isoenzyme
3o4m A 29 A 124
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 51 and 146 (29 and 124 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
3o4m
Structure name
crystal structure of porcine pancreatic phospholipase a2 in complex with 1,2-dihydroxybenzene
Structure deposition date
2010-07-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
nan
Peptide accession
P00592
Residue number A
51
Residue number B
146
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 51 of Phospholipase A2, major isoenzyme
Cysteine 146 of Phospholipase A2, major isoenzyme
3elo A 91 A 98
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 113 and 120 (91 and 98 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
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
113
Residue number B
120
Peptide name
Phospholipase A2
Ligandability
Cysteine 113 of Phospholipase A2
Cysteine 120 of Phospholipase A2
1bvm A 77 A 84
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 99 and 106 (77 and 84 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
1bvm
Structure name
solution nmr structure of bovine pancreatic phospholipase a2, 20 structures
Structure deposition date
1998-09-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00593
Residue number A
99
Residue number B
106
Peptide name
Phospholipase A2
Ligandability
Cysteine 99 of Phospholipase A2
Cysteine 106 of Phospholipase A2
1sfw A 51 A 105
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 73 and 127 (51 and 105 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
1sfw
Structure name
porcine pancreas phospholipase a2, nmr, 18 structures
Structure deposition date
1996-02-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
73
Residue number B
127
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 73 of Phospholipase A2, major isoenzyme
Cysteine 127 of Phospholipase A2, major isoenzyme
3elo A 51 A 61
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 73 and 83 (51 and 61 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
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
73
Residue number B
83
Peptide name
Phospholipase A2
Ligandability
Cysteine 73 of Phospholipase A2
Cysteine 83 of Phospholipase A2
1pir A 91 A 96
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 113 and 118 (91 and 96 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1pir
Structure name
solution structure of porcine pancreatic phospholipase a2
Structure deposition date
1994-12-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
113
Residue number B
118
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 113 of Phospholipase A2, major isoenzyme
Cysteine 118 of Phospholipase A2, major isoenzyme
1pir A 84 A 91
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 106 and 113 (84 and 91 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1pir
Structure name
solution structure of porcine pancreatic phospholipase a2
Structure deposition date
1994-12-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
106
Residue number B
113
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 106 of Phospholipase A2, major isoenzyme
Cysteine 113 of Phospholipase A2, major isoenzyme
3elo A 84 A 98
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 106 and 120 (84 and 98 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
106
Residue number B
120
Peptide name
Phospholipase A2
Ligandability
Cysteine 106 of Phospholipase A2
Cysteine 120 of Phospholipase A2
1pis A 45 A 124
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 67 and 146 (45 and 124 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
1pis
Structure name
solution structure of porcine pancreatic phospholipase a2
Structure deposition date
1994-12-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
67
Residue number B
146
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 67 of Phospholipase A2, major isoenzyme
Cysteine 146 of Phospholipase A2, major isoenzyme
3elo A 11 A 84
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 33 and 106 (11 and 84 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
33
Residue number B
106
Peptide name
Phospholipase A2
Ligandability
Cysteine 33 of Phospholipase A2
Cysteine 106 of Phospholipase A2
3elo A 11 A 96
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 33 and 118 (11 and 96 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
33
Residue number B
118
Peptide name
Phospholipase A2
Ligandability
Cysteine 33 of Phospholipase A2
Cysteine 118 of Phospholipase A2
3fvi D 96 D 98
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 118 and 120 (96 and 98 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3fvi
Structure name
crystal structure of complex of phospholipase a2 with octyl sulfates
Structure deposition date
2009-01-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
118
Residue number B
120
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 118 of Phospholipase A2, major isoenzyme
Cysteine 120 of Phospholipase A2, major isoenzyme
1bvm A 51 A 96
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 73 and 118 (51 and 96 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
1bvm
Structure name
solution nmr structure of bovine pancreatic phospholipase a2, 20 structures
Structure deposition date
1998-09-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00593
Residue number A
73
Residue number B
118
Peptide name
Phospholipase A2
Ligandability
Cysteine 73 of Phospholipase A2
Cysteine 118 of Phospholipase A2
1sfv A 44 A 98
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 66 and 120 (44 and 98 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
1sfv
Structure name
porcine pancreas phospholipase a2, nmr, minimized average structure
Structure deposition date
1996-02-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
66
Residue number B
120
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 66 of Phospholipase A2, major isoenzyme
Cysteine 120 of Phospholipase A2, major isoenzyme
1sfw A 45 A 51
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 67 and 73 (45 and 51 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
1sfw
Structure name
porcine pancreas phospholipase a2, nmr, 18 structures
Structure deposition date
1996-02-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
67
Residue number B
73
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 67 of Phospholipase A2, major isoenzyme
Cysteine 73 of Phospholipase A2, major isoenzyme
3elo A 27 A 29
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 49 and 51 (27 and 29 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
3elo
Structure name
crystal structure of human pancreatic prophospholipase a2
Structure deposition date
2008-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04054
Residue number A
49
Residue number B
51
Peptide name
Phospholipase A2
Ligandability
Cysteine 49 of Phospholipase A2
Cysteine 51 of Phospholipase A2
1pis A 98 A 105
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 120 and 127 (98 and 105 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
1pis
Structure name
solution structure of porcine pancreatic phospholipase a2
Structure deposition date
1994-12-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
120
Residue number B
127
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 120 of Phospholipase A2, major isoenzyme
Cysteine 127 of Phospholipase A2, major isoenzyme
1pis A 45 A 98
A redox-regulated disulphide may form within Phospholipase A2, major isoenzyme between cysteines 67 and 120 (45 and 98 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
1pis
Structure name
solution structure of porcine pancreatic phospholipase a2
Structure deposition date
1994-12-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00592
Residue number A
67
Residue number B
120
Peptide name
Phospholipase A2, major isoenzyme
Ligandability
Cysteine 67 of Phospholipase A2, major isoenzyme
Cysteine 120 of Phospholipase A2, major isoenzyme
1bvm A 27 A 45
A redox-regulated disulphide may form within Phospholipase A2 between cysteines 49 and 67 (27 and 45 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
1bvm
Structure name
solution nmr structure of bovine pancreatic phospholipase a2, 20 structures
Structure deposition date
1998-09-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00593
Residue number A
49
Residue number B
67
Peptide name
Phospholipase A2
Ligandability
Cysteine 49 of Phospholipase A2
Cysteine 67 of Phospholipase A2
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