ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Bone marrow proteoglycan

Intermolecular
Cysteine 169 and cysteine 732 of Pappalysin-1
Cysteine 104 and cysteine 424 of Pappalysin-1
Intramolecular
Cysteine 89 and cysteine 128
Cysteine 104 and cysteine 107
Cysteine 125 and cysteine 220
Cysteine 197 and cysteine 212
Cysteine 128 and cysteine 220
Cysteine 125 and cysteine 128
A redox-regulated disulphide may form between cysteine 169 of Bone marrow proteoglycan and cysteine 732 of Pappalysin-1 (169 and 652 respectively in this structure).

Details

Redox score ?
86
PDB code
7y5n
Structure name
structure of 1:1 papp-a
Structure deposition date
2022-06-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone marrow proteoglycan
Peptide B name
Pappalysin-1
Peptide A accession
P13727
Peptide B accession
Q13219
Peptide A residue number
169
Peptide B residue number
732

Ligandability

Cysteine 169 of Bone marrow proteoglycan

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 732 of Pappalysin-1

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 cysteine 104 of Bone marrow proteoglycan and cysteine 424 of Pappalysin-1 (104 and 344 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
7y5n
Structure name
structure of 1:1 papp-a
Structure deposition date
2022-06-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bone marrow proteoglycan
Peptide B name
Pappalysin-1
Peptide A accession
P13727
Peptide B accession
Q13219
Peptide A residue number
104
Peptide B residue number
424

Ligandability

Cysteine 104 of Bone marrow proteoglycan

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 424 of Pappalysin-1

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 Bone marrow proteoglycan between cysteines 89 and 128.

Details

Redox score ?
85
PDB code
8hgg
Structure name
structure of 2:2 papp-a
Structure deposition date
2022-11-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13727
Residue number A
89
Residue number B
128
Peptide name
Bone marrow proteoglycan

Ligandability

Cysteine 89 of Bone marrow proteoglycan

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 128 of Bone marrow proteoglycan

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 Bone marrow proteoglycan between cysteines 104 and 107.

Details

Redox score ?
85
PDB code
8hgg
Structure name
structure of 2:2 papp-a
Structure deposition date
2022-11-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13727
Residue number A
104
Residue number B
107
Peptide name
Bone marrow proteoglycan

Ligandability

Cysteine 104 of Bone marrow proteoglycan

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 107 of Bone marrow proteoglycan

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 Bone marrow proteoglycan between cysteines 125 and 220 (20 and 115 respectively in this structure).

Details

Redox score ?
85
PDB code
2brs
Structure name
embp heparin complex
Structure deposition date
2005-05-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13727
Residue number A
125
Residue number B
220
Peptide name
Bone marrow proteoglycan

Ligandability

Cysteine 125 of Bone marrow proteoglycan

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 220 of Bone marrow proteoglycan

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 Bone marrow proteoglycan between cysteines 197 and 212 (92 and 107 respectively in this structure).

Details

Redox score ?
84
PDB code
1h8u
Structure name
crystal structure of the eosinophil major basic protein at 1
Structure deposition date
2001-02-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13727
Residue number A
197
Residue number B
212
Peptide name
Bone marrow proteoglycan

Ligandability

Cysteine 197 of Bone marrow proteoglycan

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 212 of Bone marrow proteoglycan

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 Bone marrow proteoglycan between cysteines 128 and 220 (23 and 115 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
2brs
Structure name
embp heparin complex
Structure deposition date
2005-05-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
nan
Peptide accession
P13727
Residue number A
128
Residue number B
220
Peptide name
Bone marrow proteoglycan

Ligandability

Cysteine 128 of Bone marrow proteoglycan

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 220 of Bone marrow proteoglycan

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 Bone marrow proteoglycan between cysteines 125 and 128 (20 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2brs
Structure name
embp heparin complex
Structure deposition date
2005-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
nan
Peptide accession
P13727
Residue number A
125
Residue number B
128
Peptide name
Bone marrow proteoglycan

Ligandability

Cysteine 125 of Bone marrow proteoglycan

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 128 of Bone marrow proteoglycan

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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