ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Egl nine homolog 1

Intermolecular
Cysteine 201 and cysteine 780 of Hypoxia-inducible factor 1-alpha L
Intramolecular
Cysteine 201 and cysteine 208
Cysteine 208 and cysteine 283
Cysteine 283 and cysteine 326
Cysteine 208 and cysteine 326
Cysteine 323 and cysteine 326
Cysteine 21 and cysteine 283
A redox-regulated disulphide may form between cysteine 201 of Egl nine homolog 1 and cysteine 780 of Hypoxia-inducible factor 1-alpha (314 and 397 respectively in this structure).

Details

Redox score ?
81
PDB code
5la9
Structure name
hif prolyl hydroxylase 2 (phd2-r281c/v314c) cross-linked to hif-1alpha nodd-l397c/d412c and n-oxalylglycine (nog) (complex-2)
Structure deposition date
2016-06-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
Egl nine homolog 1
Peptide B name
Hypoxia-inducible factor 1-alpha
Peptide A accession
Q9GZT9
Peptide B accession
Q16665
Peptide A residue number
201
Peptide B residue number
780

Ligandability

Cysteine 201 of Egl nine homolog 1

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 780 of Hypoxia-inducible factor 1-alpha

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.

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 397 has been assigned to correct residue.
A redox-regulated disulphide may form within Egl nine homolog 1 between cysteines 201 and 208.

Details

Redox score ?
70
PDB code
6st3
Structure name
hif prolyl hydroxylase 2 (phd2/ egln1) in complex with 4-hydroxy-n-(4- phenoxybenzyl)-2-(1h-pyrazol-1-yl)pyrimidine-5-carboxamide
Structure deposition date
2019-09-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
54
Peptide accession
Q9GZT9
Residue number A
201
Residue number B
208
Peptide name
Egl nine homolog 1

Ligandability

Cysteine 201 of Egl nine homolog 1

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 208 of Egl nine homolog 1

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 Egl nine homolog 1 between cysteines 208 and 283. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3hqr
Structure name
phd2:mn:nog:hif1-alpha substrate complex
Structure deposition date
2009-06-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
62
Peptide accession
Q9GZT9
Residue number A
208
Residue number B
283
Peptide name
Egl nine homolog 1

Ligandability

Cysteine 208 of Egl nine homolog 1

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 283 of Egl nine homolog 1

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 Egl nine homolog 1 between cysteines 283 and 326. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3ouj
Structure name
phd2 with 2-oxoglutarate
Structure deposition date
2010-09-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
87
Peptide accession
Q9GZT9
Residue number A
283
Residue number B
326
Peptide name
Egl nine homolog 1

Ligandability

Cysteine 283 of Egl nine homolog 1

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 326 of Egl nine homolog 1

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 Egl nine homolog 1 between cysteines 208 and 326. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
7ump
Structure name
crystal structure of phd2 catalytic domain (cid 7465) in complex with akb-6548 at 1
Structure deposition date
2022-04-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
84
Peptide accession
Q9GZT9
Residue number A
208
Residue number B
326
Peptide name
Egl nine homolog 1

Ligandability

Cysteine 208 of Egl nine homolog 1

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 326 of Egl nine homolog 1

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 Egl nine homolog 1 between cysteines 323 and 326. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
5l9v
Structure name
hif prolyl hydroxylase 2 (phd2-r281c/p317c) cross-linked to hif-1alpha nodd-l397c/d412c and n-oxalylglycine (nog) (complex-1)
Structure deposition date
2016-06-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
Q9GZT9
Residue number A
323
Residue number B
326
Peptide name
Egl nine homolog 1

Ligandability

Cysteine 323 of Egl nine homolog 1

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 326 of Egl nine homolog 1

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 Egl nine homolog 1 between cysteines 21 and 283 (281 and 283 respectively in this structure).

Details

Redox score ?
nan
PDB code
5las
Structure name
hif prolyl hydroxylase 2 (phd2-r281c/p317c/r396t) cross-linked to hif- 1alpha nodd-l397c/d412c and n-oxalylglycine (nog) (complex-3)
Structure deposition date
2016-06-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9GZT9
Residue number A
21
Residue number B
283
Peptide name
Egl nine homolog 1

Ligandability

Cysteine 21 of Egl nine homolog 1

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 283 of Egl nine homolog 1

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 281 has been assigned to correct residue.
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