ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Hemopexin

Intramolecular
Cysteine 52 and cysteine 233
Cysteine 255 and cysteine 458
Cysteine 151 and cysteine 156
Cysteine 364 and cysteine 406
Cysteine 416 and cysteine 433
Cysteine 190 and cysteine 202
Cysteine 406 and cysteine 433
Cysteine 406 and cysteine 416
A redox-regulated disulphide may form within Hemopexin between cysteines 52 and 233 (27 and 208 respectively in this structure).

Details

Redox score ?
90
PDB code
4rt6
Structure name
structure of a complex between hemopexin and hemopexin binding protein
Structure deposition date
2014-11-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20058
Residue number A
52
Residue number B
233
Peptide name
Hemopexin

Ligandability

Cysteine 52 of Hemopexin

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 233 of Hemopexin

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 Hemopexin between cysteines 255 and 458 (230 and 433 respectively in this structure).

Details

Redox score ?
86
PDB code
1qjs
Structure name
mammalian blood serum haemopexin glycosylated-native protein and in complex with its ligand haem
Structure deposition date
1999-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20058
Residue number A
255
Residue number B
458
Peptide name
Hemopexin

Ligandability

Cysteine 255 of Hemopexin

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 458 of Hemopexin

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 Hemopexin between cysteines 151 and 156 (126 and 131 respectively in this structure).

Details

Redox score ?
85
PDB code
4rt6
Structure name
structure of a complex between hemopexin and hemopexin binding protein
Structure deposition date
2014-11-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20058
Residue number A
151
Residue number B
156
Peptide name
Hemopexin

Ligandability

Cysteine 151 of Hemopexin

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 156 of Hemopexin

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 Hemopexin between cysteines 364 and 406 (339 and 381 respectively in this structure).

Details

Redox score ?
80
PDB code
1qjs
Structure name
mammalian blood serum haemopexin glycosylated-native protein and in complex with its ligand haem
Structure deposition date
1999-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20058
Residue number A
364
Residue number B
406
Peptide name
Hemopexin

Ligandability

Cysteine 364 of Hemopexin

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 406 of Hemopexin

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 Hemopexin between cysteines 416 and 433 (391 and 408 respectively in this structure).

Details

Redox score ?
80
PDB code
1qjs
Structure name
mammalian blood serum haemopexin glycosylated-native protein and in complex with its ligand haem
Structure deposition date
1999-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20058
Residue number A
416
Residue number B
433
Peptide name
Hemopexin

Ligandability

Cysteine 416 of Hemopexin

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 433 of Hemopexin

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 Hemopexin between cysteines 190 and 202 (165 and 177 respectively in this structure).

Details

Redox score ?
80
PDB code
1qhu
Structure name
mammalian blood serum haemopexin deglycosylated and in complex with its ligand haem
Structure deposition date
1999-05-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20058
Residue number A
190
Residue number B
202
Peptide name
Hemopexin

Ligandability

Cysteine 190 of Hemopexin

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 202 of Hemopexin

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 Hemopexin between cysteines 406 and 433 (380 and 407 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
1hxn
Structure name
1
Structure deposition date
1995-06-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20058
Residue number A
406
Residue number B
433
Peptide name
Hemopexin

Ligandability

Cysteine 406 of Hemopexin

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 433 of Hemopexin

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 Hemopexin between cysteines 406 and 416 (380 and 390 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
1hxn
Structure name
1
Structure deposition date
1995-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P20058
Residue number A
406
Residue number B
416
Peptide name
Hemopexin

Ligandability

Cysteine 406 of Hemopexin

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 416 of Hemopexin

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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