ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Inositol polyphosphate 5-phosphatase OCRL

Intramolecular
Cysteine 82 and cysteine 104
Cysteine 688 and cysteine 831
Cysteine 811 and cysteine 821
Cysteine 804 and cysteine 831
Cysteine 64 and cysteine 104
Cysteine 679 and cysteine 771
Cysteine 64 and cysteine 82
Cysteine 370 and cysteine 394
Cysteine 804 and cysteine 811
A redox-regulated disulphide may form within Inositol polyphosphate 5-phosphatase OCRL between cysteines 82 and 104 (87 and 109 respectively in this structure).

Details

Redox score ?
85
PDB code
2kie
Structure name
a ph domain within ocrl bridges clathrin mediated membrane trafficking to phosphoinositide metabolis
Structure deposition date
2009-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q01968
Residue number A
82
Residue number B
104
Peptide name
Inositol polyphosphate 5-phosphatase OCRL

Ligandability

Cysteine 82 of Inositol polyphosphate 5-phosphatase OCRL

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 104 of Inositol polyphosphate 5-phosphatase OCRL

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 Inositol polyphosphate 5-phosphatase OCRL between cysteines 688 and 831 (129 and 272 respectively in this structure).

Details

Redox score ?
75
PDB code
2qv2
Structure name
a role of the lowe syndrome protein ocrl in early steps of the endocytic pathway
Structure deposition date
2007-08-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
50
Peptide accession
Q01968
Residue number A
688
Residue number B
831
Peptide name
Inositol polyphosphate 5-phosphatase OCRL

Ligandability

Cysteine 688 of Inositol polyphosphate 5-phosphatase OCRL

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 831 of Inositol polyphosphate 5-phosphatase OCRL

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 Inositol polyphosphate 5-phosphatase OCRL between cysteines 811 and 821 (252 and 262 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
2qv2
Structure name
a role of the lowe syndrome protein ocrl in early steps of the endocytic pathway
Structure deposition date
2007-08-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
64
Peptide accession
Q01968
Residue number A
811
Residue number B
821
Peptide name
Inositol polyphosphate 5-phosphatase OCRL

Ligandability

Cysteine 811 of Inositol polyphosphate 5-phosphatase OCRL

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 821 of Inositol polyphosphate 5-phosphatase OCRL

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 Inositol polyphosphate 5-phosphatase OCRL between cysteines 804 and 831. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
3qis
Structure name
recognition of the f&h motif by the lowe syndrome protein ocrl
Structure deposition date
2011-01-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
52
Peptide accession
Q01968
Residue number A
804
Residue number B
831
Peptide name
Inositol polyphosphate 5-phosphatase OCRL

Ligandability

Cysteine 804 of Inositol polyphosphate 5-phosphatase OCRL

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 831 of Inositol polyphosphate 5-phosphatase OCRL

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 Inositol polyphosphate 5-phosphatase OCRL between cysteines 64 and 104 (69 and 109 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
2kie
Structure name
a ph domain within ocrl bridges clathrin mediated membrane trafficking to phosphoinositide metabolis
Structure deposition date
2009-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
nan
Peptide accession
Q01968
Residue number A
64
Residue number B
104
Peptide name
Inositol polyphosphate 5-phosphatase OCRL

Ligandability

Cysteine 64 of Inositol polyphosphate 5-phosphatase OCRL

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 104 of Inositol polyphosphate 5-phosphatase OCRL

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 Inositol polyphosphate 5-phosphatase OCRL between cysteines 679 and 771. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3qis
Structure name
recognition of the f&h motif by the lowe syndrome protein ocrl
Structure deposition date
2011-01-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
76
Peptide accession
Q01968
Residue number A
679
Residue number B
771
Peptide name
Inositol polyphosphate 5-phosphatase OCRL

Ligandability

Cysteine 679 of Inositol polyphosphate 5-phosphatase OCRL

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 771 of Inositol polyphosphate 5-phosphatase OCRL

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 Inositol polyphosphate 5-phosphatase OCRL between cysteines 64 and 82 (69 and 87 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
2kie
Structure name
a ph domain within ocrl bridges clathrin mediated membrane trafficking to phosphoinositide metabolis
Structure deposition date
2009-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
nan
Peptide accession
Q01968
Residue number A
64
Residue number B
82
Peptide name
Inositol polyphosphate 5-phosphatase OCRL

Ligandability

Cysteine 64 of Inositol polyphosphate 5-phosphatase OCRL

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 82 of Inositol polyphosphate 5-phosphatase OCRL

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 Inositol polyphosphate 5-phosphatase OCRL between cysteines 370 and 394. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4cmn
Structure name
crystal structure of ocrl in complex with a phosphate ion
Structure deposition date
2014-01-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
86
Peptide accession
Q01968
Residue number A
370
Residue number B
394
Peptide name
Inositol polyphosphate 5-phosphatase OCRL

Ligandability

Cysteine 370 of Inositol polyphosphate 5-phosphatase OCRL

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 394 of Inositol polyphosphate 5-phosphatase OCRL

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 Inositol polyphosphate 5-phosphatase OCRL between cysteines 804 and 811 (245 and 252 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
2qv2
Structure name
a role of the lowe syndrome protein ocrl in early steps of the endocytic pathway
Structure deposition date
2007-08-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
66
Peptide accession
Q01968
Residue number A
804
Residue number B
811
Peptide name
Inositol polyphosphate 5-phosphatase OCRL

Ligandability

Cysteine 804 of Inositol polyphosphate 5-phosphatase OCRL

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 811 of Inositol polyphosphate 5-phosphatase OCRL

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.

If this tool was useful for finding a disulphide, please cite: