ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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B-cell CLL/lymphoma 9-like protein

Intramolecular
Cysteine 1216 and cysteine 333
Cysteine 1216 and cysteine 358
Cysteine 1216 and cysteine 379
Cysteine 333 and cysteine 358
Cysteine 379 and cysteine 382
Cysteine 350 and cysteine 382
Cysteine 346 and cysteine 382
Cysteine 350 and cysteine 379
Cysteine 346 and cysteine 350
A redox-regulated disulphide may form within B-cell CLL/lymphoma 9-like protein between cysteines 1216 and 333 (330 and 333 respectively in this structure).

Details

Redox score ?
nan
PDB code
4up0
Structure name
ternary crystal structure of the pygo2 phd finger in complex with the b9l hd1 domain and a h3k4me2 peptide
Structure deposition date
2014-06-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
11
Peptide accession
Q86UU0
Residue number A
1216
Residue number B
333
Peptide name
B-cell CLL/lymphoma 9-like protein

Ligandability

Cysteine 1216 of B-cell CLL/lymphoma 9-like protein

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 333 of B-cell CLL/lymphoma 9-like protein

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.

Uncertain whether structure cysteine 330 has been assigned to correct residue.
Cysteine 333 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within B-cell CLL/lymphoma 9-like protein between cysteines 1216 and 358 (330 and 358 respectively in this structure).

Details

Redox score ?
nan
PDB code
4up0
Structure name
ternary crystal structure of the pygo2 phd finger in complex with the b9l hd1 domain and a h3k4me2 peptide
Structure deposition date
2014-06-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
16
Peptide accession
Q86UU0
Residue number A
1216
Residue number B
358
Peptide name
B-cell CLL/lymphoma 9-like protein

Ligandability

Cysteine 1216 of B-cell CLL/lymphoma 9-like protein

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 358 of B-cell CLL/lymphoma 9-like protein

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.

Uncertain whether structure cysteine 330 has been assigned to correct residue.
Cysteine 358 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within B-cell CLL/lymphoma 9-like protein between cysteines 1216 and 379 (330 and 379 respectively in this structure).

Details

Redox score ?
nan
PDB code
4up5
Structure name
crystal structure of the pygo2 phd finger in complex with the b9l hd1 domain and a chemical fragment
Structure deposition date
2014-06-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
5
% buried
18
Peptide accession
Q86UU0
Residue number A
1216
Residue number B
379
Peptide name
B-cell CLL/lymphoma 9-like protein

Ligandability

Cysteine 1216 of B-cell CLL/lymphoma 9-like protein

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 379 of B-cell CLL/lymphoma 9-like protein

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.

Uncertain whether structure cysteine 330 has been assigned to correct residue.
Cysteine 379 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within B-cell CLL/lymphoma 9-like protein between cysteines 333 and 358.

Details

Redox score ?
nan
PDB code
2xb1
Structure name
crystal structure of the human pygo2 phd finger in complex with the b9l hd1 domain
Structure deposition date
2010-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
2
Peptide accession
Q86UU0
Residue number A
333
Residue number B
358
Peptide name
B-cell CLL/lymphoma 9-like protein

Ligandability

Cysteine 333 of B-cell CLL/lymphoma 9-like protein

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 358 of B-cell CLL/lymphoma 9-like protein

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 333 in protein A could not be asigned to a Uniprot residue.
Cysteine 358 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within B-cell CLL/lymphoma 9-like protein between cysteines 379 and 382.

Details

Redox score ?
nan
PDB code
2xb1
Structure name
crystal structure of the human pygo2 phd finger in complex with the b9l hd1 domain
Structure deposition date
2010-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
13
Peptide accession
Q86UU0
Residue number A
379
Residue number B
382
Peptide name
B-cell CLL/lymphoma 9-like protein

Ligandability

Cysteine 379 of B-cell CLL/lymphoma 9-like protein

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 382 of B-cell CLL/lymphoma 9-like protein

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 379 in protein A could not be asigned to a Uniprot residue.
Cysteine 382 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within B-cell CLL/lymphoma 9-like protein between cysteines 350 and 382.

Details

Redox score ?
nan
PDB code
4up0
Structure name
ternary crystal structure of the pygo2 phd finger in complex with the b9l hd1 domain and a h3k4me2 peptide
Structure deposition date
2014-06-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
7
% buried
4
Peptide accession
Q86UU0
Residue number A
350
Residue number B
382
Peptide name
B-cell CLL/lymphoma 9-like protein

Ligandability

Cysteine 350 of B-cell CLL/lymphoma 9-like protein

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 382 of B-cell CLL/lymphoma 9-like protein

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 350 in protein A could not be asigned to a Uniprot residue.
Cysteine 382 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within B-cell CLL/lymphoma 9-like protein between cysteines 346 and 382.

Details

Redox score ?
nan
PDB code
4up5
Structure name
crystal structure of the pygo2 phd finger in complex with the b9l hd1 domain and a chemical fragment
Structure deposition date
2014-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
6
% buried
10
Peptide accession
Q86UU0
Residue number A
346
Residue number B
382
Peptide name
B-cell CLL/lymphoma 9-like protein

Ligandability

Cysteine 346 of B-cell CLL/lymphoma 9-like protein

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 382 of B-cell CLL/lymphoma 9-like protein

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 346 in protein A could not be asigned to a Uniprot residue.
Cysteine 382 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within B-cell CLL/lymphoma 9-like protein between cysteines 350 and 379.

Details

Redox score ?
nan
PDB code
2xb1
Structure name
crystal structure of the human pygo2 phd finger in complex with the b9l hd1 domain
Structure deposition date
2010-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
22
Peptide accession
Q86UU0
Residue number A
350
Residue number B
379
Peptide name
B-cell CLL/lymphoma 9-like protein

Ligandability

Cysteine 350 of B-cell CLL/lymphoma 9-like protein

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 379 of B-cell CLL/lymphoma 9-like protein

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 350 in protein A could not be asigned to a Uniprot residue.
Cysteine 379 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within B-cell CLL/lymphoma 9-like protein between cysteines 346 and 350.

Details

Redox score ?
nan
PDB code
4up0
Structure name
ternary crystal structure of the pygo2 phd finger in complex with the b9l hd1 domain and a h3k4me2 peptide
Structure deposition date
2014-06-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
18
Peptide accession
Q86UU0
Residue number A
346
Residue number B
350
Peptide name
B-cell CLL/lymphoma 9-like protein

Ligandability

Cysteine 346 of B-cell CLL/lymphoma 9-like protein

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 350 of B-cell CLL/lymphoma 9-like protein

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 346 in protein A could not be asigned to a Uniprot residue.
Cysteine 350 in protein B could not be asigned to a Uniprot residue.
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