ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Heterogeneous nuclear ribonucleoprotein L

Intramolecular
Cysteine 260 and cysteine 261
Cysteine 430 and cysteine 506
Cysteine 215 and cysteine 218 L
Cysteine 404 and cysteine 581 L
A redox-regulated disulphide may form within Heterogeneous nuclear ribonucleoprotein L between cysteines 260 and 261.

Details

Redox score ?
71
PDB code
7evr
Structure name
crystal structure of hnrnp l rrm2 in complex with setd2
Structure deposition date
2021-05-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
28
Peptide accession
P14866
Residue number A
260
Residue number B
261
Peptide name
Heterogeneous nuclear ribonucleoprotein L

Ligandability

Cysteine 260 of Heterogeneous nuclear ribonucleoprotein L

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 261 of Heterogeneous nuclear ribonucleoprotein L

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 Heterogeneous nuclear ribonucleoprotein L between cysteines 430 and 506 (393 and 469 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
4qpt
Structure name
structural investigation of hnrnp l
Structure deposition date
2014-06-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
36
Peptide accession
Q5U1Y5
Residue number A
430
Residue number B
506
Peptide name
Heterogeneous nuclear ribonucleoprotein L

Ligandability

Cysteine 430 of Heterogeneous nuclear ribonucleoprotein L

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 506 of Heterogeneous nuclear ribonucleoprotein L

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 Heterogeneous nuclear ribonucleoprotein L between cysteines 215 and 218. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7evr
Structure name
crystal structure of hnrnp l rrm2 in complex with setd2
Structure deposition date
2021-05-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
84
Peptide accession
P14866
Residue number A
215
Residue number B
218
Peptide name
Heterogeneous nuclear ribonucleoprotein L

Ligandability

Cysteine 215 of Heterogeneous nuclear ribonucleoprotein L

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 218 of Heterogeneous nuclear ribonucleoprotein L

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Heterogeneous nuclear ribonucleoprotein L between cysteines 404 and 581. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3to8
Structure name
crystal structure of the two c-terminal rrm domains of heterogeneous nuclear ribonucleoprotein l (hnrnp l)
Structure deposition date
2011-09-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
10
% buried
90
Peptide accession
P14866
Residue number A
404
Residue number B
581
Peptide name
Heterogeneous nuclear ribonucleoprotein L

Ligandability

Cysteine 404 of Heterogeneous nuclear ribonucleoprotein L

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 581 of Heterogeneous nuclear ribonucleoprotein L

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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