ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prostate-specific antigen

Intramolecular
Cysteine 152 and cysteine 219
Cysteine 31 and cysteine 173
Cysteine 184 and cysteine 198
Cysteine 209 and cysteine 234
Cysteine 50 and cysteine 66
A redox-regulated disulphide may form within Prostate-specific antigen between cysteines 152 and 219 (136 and 201 respectively in this structure).

Details

Redox score ?
84
PDB code
3qum
Structure name
crystal structure of human prostate specific antigen (psa) in fab sandwich with a high affinity and a pca selective antibody
Structure deposition date
2011-02-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07288
Residue number A
152
Residue number B
219
Peptide name
Prostate-specific antigen

Ligandability

Cysteine 152 of Prostate-specific antigen

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 219 of Prostate-specific antigen

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 Prostate-specific antigen between cysteines 31 and 173 (22 and 157 respectively in this structure).

Details

Redox score ?
82
PDB code
3qum
Structure name
crystal structure of human prostate specific antigen (psa) in fab sandwich with a high affinity and a pca selective antibody
Structure deposition date
2011-02-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07288
Residue number A
31
Residue number B
173
Peptide name
Prostate-specific antigen

Ligandability

Cysteine 31 of Prostate-specific antigen

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 173 of Prostate-specific antigen

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 Prostate-specific antigen between cysteines 184 and 198 (168 and 182 respectively in this structure).

Details

Redox score ?
82
PDB code
3qum
Structure name
crystal structure of human prostate specific antigen (psa) in fab sandwich with a high affinity and a pca selective antibody
Structure deposition date
2011-02-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07288
Residue number A
184
Residue number B
198
Peptide name
Prostate-specific antigen

Ligandability

Cysteine 184 of Prostate-specific antigen

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 198 of Prostate-specific antigen

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 Prostate-specific antigen between cysteines 209 and 234 (191 and 220 respectively in this structure).

Details

Redox score ?
82
PDB code
3qum
Structure name
crystal structure of human prostate specific antigen (psa) in fab sandwich with a high affinity and a pca selective antibody
Structure deposition date
2011-02-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07288
Residue number A
209
Residue number B
234
Peptide name
Prostate-specific antigen

Ligandability

Cysteine 209 of Prostate-specific antigen

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 234 of Prostate-specific antigen

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 Prostate-specific antigen between cysteines 50 and 66 (42 and 58 respectively in this structure).

Details

Redox score ?
78
PDB code
3qum
Structure name
crystal structure of human prostate specific antigen (psa) in fab sandwich with a high affinity and a pca selective antibody
Structure deposition date
2011-02-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07288
Residue number A
50
Residue number B
66
Peptide name
Prostate-specific antigen

Ligandability

Cysteine 50 of Prostate-specific antigen

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 66 of Prostate-specific antigen

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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