ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Phospholipase A2, membrane associated

Intermolecular
Cysteine 103 and cysteine 103
Cysteine 103 and cysteine 79
Cysteine 79 and cysteine 79
Intramolecular
Cysteine 69 and cysteine 144
Cysteine 97 and cysteine 108
Cysteine 46 and cysteine 137
Cysteine 70 and cysteine 110
Cysteine 48 and cysteine 64
Cysteine 63 and cysteine 117
Cysteine 63 and cysteine 64
More...
Cysteine 48 and cysteine 63
Cysteine 79 and cysteine 110
Cysteine 70 and cysteine 144
Cysteine 64 and cysteine 117
Cysteine 48 and cysteine 117
Cysteine 48 and cysteine 137
Cysteine 46 and cysteine 48
Cysteine 69 and cysteine 70
Cysteine 110 and cysteine 144
Cysteine 97 and cysteine 110
Cysteine 69 and cysteine 110
Cysteine 108 and cysteine 110
Cysteine 70 and cysteine 79
Cysteine 46 and cysteine 64
A redox-regulated disulphide may form between two units of Phospholipase A2, membrane associated at cysteines 103 and 103 (83 and 83 respectively in this structure).

Details

Redox score ?
62
PDB code
1ayp
Structure name
a probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement
Structure deposition date
1994-07-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Phospholipase A2, membrane associated
Peptide B name
Phospholipase A2, membrane associated
Peptide A accession
P14555
Peptide B accession
P14555
Peptide A residue number
103
Peptide B residue number
103

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between two units of Phospholipase A2, membrane associated at cysteines 103 and 79 (83 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 ?
57
PDB code
1ayp
Structure name
a probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement
Structure deposition date
1994-07-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Phospholipase A2, membrane associated
Peptide B name
Phospholipase A2, membrane associated
Peptide A accession
P14555
Peptide B accession
P14555
Peptide A residue number
103
Peptide B residue number
79

Ligandability

Cysteine 103 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 79 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between two units of Phospholipase A2, membrane associated at cysteines 79 and 79 (59 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 ?
47
PDB code
1ayp
Structure name
a probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement
Structure deposition date
1994-07-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Phospholipase A2, membrane associated
Peptide B name
Phospholipase A2, membrane associated
Peptide A accession
P14555
Peptide B accession
P14555
Peptide A residue number
79
Peptide B residue number
79

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 69 and 144 (49 and 124 respectively in this structure).

Details

Redox score ?
86
PDB code
1kvo
Structure name
human phospholipase a2 complexed with a highly potent substrate anologue
Structure deposition date
1996-07-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
69
Residue number B
144
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 69 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 144 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 97 and 108 (77 and 88 respectively in this structure).

Details

Redox score ?
83
PDB code
1db5
Structure name
human s-pla2 in complex with indole 6
Structure deposition date
1999-11-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
97
Residue number B
108
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 97 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 108 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 46 and 137 (26 and 117 respectively in this structure).

Details

Redox score ?
82
PDB code
1ayp
Structure name
a probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement
Structure deposition date
1994-07-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
46
Residue number B
137
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 46 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 137 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 70 and 110 (50 and 90 respectively in this structure).

Details

Redox score ?
81
PDB code
3u8h
Structure name
functionally selective inhibition of group iia phospholipase a2 reveals a role for vimentin in regulating arachidonic acid metabolism
Structure deposition date
2011-10-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
70
Residue number B
110
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 70 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 110 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 48 and 64 (28 and 44 respectively in this structure).

Details

Redox score ?
80
PDB code
3u8d
Structure name
functionally selective inhibition of group iia phospholipase a2 reveals a role for vimentin in regulating arachidonic acid metabolism
Structure deposition date
2011-10-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
48
Residue number B
64
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 48 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 64 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 63 and 117 (43 and 97 respectively in this structure).

Details

Redox score ?
80
PDB code
3u8d
Structure name
functionally selective inhibition of group iia phospholipase a2 reveals a role for vimentin in regulating arachidonic acid metabolism
Structure deposition date
2011-10-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
63
Residue number B
117
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 63 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 117 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 63 and 64 (43 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 ?
54
PDB code
3u8i
Structure name
functionally selective inhibition of group iia phospholipase a2 reveals a role for vimentin in regulating arachidonic acid metabolism
Structure deposition date
2011-10-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
63
Residue number B
64
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 63 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 64 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 48 and 63 (28 and 43 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
1n28
Structure name
crystal structure of the h48q mutant of human group iia phospholipase a2
Structure deposition date
2002-10-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
48
Residue number B
63
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 48 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 63 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 79 and 110 (59 and 90 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
1j1a
Structure name
pancreatic secretory phospholipase a2 (iia) with anti- inflammatory activity
Structure deposition date
2002-12-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
79
Residue number B
110
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 79 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 110 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 70 and 144 (50 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
1kvo
Structure name
human phospholipase a2 complexed with a highly potent substrate anologue
Structure deposition date
1996-07-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
70
Residue number B
144
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 70 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 144 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 64 and 117 (44 and 97 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
1pod
Structure name
structures of free and inhibited human secretory phospholipase a2 from inflammatory exudate
Structure deposition date
1992-09-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
64
Residue number B
117
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 64 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 117 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 48 and 117 (28 and 97 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
1n28
Structure name
crystal structure of the h48q mutant of human group iia phospholipase a2
Structure deposition date
2002-10-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
48
Residue number B
117
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 48 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 117 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 48 and 137 (28 and 117 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
3u8h
Structure name
functionally selective inhibition of group iia phospholipase a2 reveals a role for vimentin in regulating arachidonic acid metabolism
Structure deposition date
2011-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
48
Residue number B
137
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 48 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 137 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 46 and 48 (26 and 28 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
1ayp
Structure name
a probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement
Structure deposition date
1994-07-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
46
Residue number B
48
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 46 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 48 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 69 and 70 (49 and 50 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
1pod
Structure name
structures of free and inhibited human secretory phospholipase a2 from inflammatory exudate
Structure deposition date
1992-09-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
69
Residue number B
70
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 69 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 70 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 110 and 144 (90 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
5g3n
Structure name
discovery of a novel secreted phospholipase a2 (spla2) inhibitor
Structure deposition date
2016-04-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
110
Residue number B
144
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 110 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 144 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 97 and 110 (77 and 90 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
1ayp
Structure name
a probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement
Structure deposition date
1994-07-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
97
Residue number B
110
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 97 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 110 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 69 and 110 (49 and 90 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
5g3n
Structure name
discovery of a novel secreted phospholipase a2 (spla2) inhibitor
Structure deposition date
2016-04-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
69
Residue number B
110
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 69 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 110 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 108 and 110 (88 and 90 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
1kvo
Structure name
human phospholipase a2 complexed with a highly potent substrate anologue
Structure deposition date
1996-07-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
108
Residue number B
110
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 108 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 110 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 70 and 79 (50 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 ?
37
PDB code
1kvo
Structure name
human phospholipase a2 complexed with a highly potent substrate anologue
Structure deposition date
1996-07-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
70
Residue number B
79
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 70 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 79 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Phospholipase A2, membrane associated between cysteines 46 and 64 (26 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 ?
36
PDB code
1pod
Structure name
structures of free and inhibited human secretory phospholipase a2 from inflammatory exudate
Structure deposition date
1992-09-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14555
Residue number A
46
Residue number B
64
Peptide name
Phospholipase A2, membrane associated

Ligandability

Cysteine 46 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 64 of Phospholipase A2, membrane associated

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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