ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Hypoxia-inducible factor 1-alpha

Intermolecular
Cysteine 201 of Egl nine homolog 1 and cysteine 780 L
Cysteine 379 of Histone lysine acetyltransferase CREBBP and cysteine 780 L
Cysteine 366 of Histone lysine acetyltransferase CREBBP and cysteine 780 L
Cysteine 384 of Histone lysine acetyltransferase CREBBP and cysteine 780 L
Cysteine 429 of Histone lysine acetyltransferase CREBBP and cysteine 780 L
Cysteine 800 and cysteine 414 of Histone acetyltransferase p300
Intramolecular
Cysteine 334 and cysteine 337
Cysteine 255 and cysteine 337
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 between cysteine 379 of Histone lysine acetyltransferase CREBBP and cysteine 780 of Hypoxia-inducible factor 1-alpha (35 and 103 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
1l8c
Structure name
structural basis for hif-1alpha/cbp recognition in the cellular hypoxic response
Structure deposition date
2002-03-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
32
Peptide A name
Histone lysine acetyltransferase CREBBP
Peptide B name
Hypoxia-inducible factor 1-alpha
Peptide A accession
P45481
Peptide B accession
Q16665
Peptide A residue number
379
Peptide B residue number
780

Ligandability

Cysteine 379 of Histone lysine acetyltransferase CREBBP

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.

A redox-regulated disulphide may form between cysteine 366 of Histone lysine acetyltransferase CREBBP and cysteine 780 of Hypoxia-inducible factor 1-alpha (22 and 103 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
1l8c
Structure name
structural basis for hif-1alpha/cbp recognition in the cellular hypoxic response
Structure deposition date
2002-03-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
36
Peptide A name
Histone lysine acetyltransferase CREBBP
Peptide B name
Hypoxia-inducible factor 1-alpha
Peptide A accession
P45481
Peptide B accession
Q16665
Peptide A residue number
366
Peptide B residue number
780

Ligandability

Cysteine 366 of Histone lysine acetyltransferase CREBBP

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.

A redox-regulated disulphide may form between cysteine 384 of Histone lysine acetyltransferase CREBBP and cysteine 780 of Hypoxia-inducible factor 1-alpha (40 and 103 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
1l8c
Structure name
structural basis for hif-1alpha/cbp recognition in the cellular hypoxic response
Structure deposition date
2002-03-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
44
Peptide A name
Histone lysine acetyltransferase CREBBP
Peptide B name
Hypoxia-inducible factor 1-alpha
Peptide A accession
P45481
Peptide B accession
Q16665
Peptide A residue number
384
Peptide B residue number
780

Ligandability

Cysteine 384 of Histone lysine acetyltransferase CREBBP

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.

A redox-regulated disulphide may form between cysteine 429 of Histone lysine acetyltransferase CREBBP and cysteine 780 of Hypoxia-inducible factor 1-alpha (85 and 103 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1l8c
Structure name
structural basis for hif-1alpha/cbp recognition in the cellular hypoxic response
Structure deposition date
2002-03-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
52
Peptide A name
Histone lysine acetyltransferase CREBBP
Peptide B name
Hypoxia-inducible factor 1-alpha
Peptide A accession
P45481
Peptide B accession
Q16665
Peptide A residue number
429
Peptide B residue number
780

Ligandability

Cysteine 429 of Histone lysine acetyltransferase CREBBP

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 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.

A redox-regulated disulphide may form between cysteine 800 of Hypoxia-inducible factor 1-alpha and cysteine 414 of Histone acetyltransferase p300 (16 and 192 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
1l3e
Structure name
nmr structures of the hif-1alpha ctad/p300 ch1 complex
Structure deposition date
2002-02-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
70
Peptide A name
Hypoxia-inducible factor 1-alpha
Peptide B name
Histone acetyltransferase p300
Peptide A accession
Q16665
Peptide B accession
Q09472
Peptide A residue number
800
Peptide B residue number
414

Ligandability

Cysteine 800 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.

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 414 of Histone acetyltransferase p300

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 Hypoxia-inducible factor 1-alpha between cysteines 334 and 337. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
4h6j
Structure name
identification of cys 255 in hif-1 as a novel site for development of covalent inhibitors of hif-1 /arnt pasb domain protein-protein interaction
Structure deposition date
2012-09-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
96
Peptide accession
Q16665
Residue number A
334
Residue number B
337
Peptide name
Hypoxia-inducible factor 1-alpha

Ligandability

Cysteine 334 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.

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 337 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.

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 Hypoxia-inducible factor 1-alpha between cysteines 255 and 337. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
4h6j
Structure name
identification of cys 255 in hif-1 as a novel site for development of covalent inhibitors of hif-1 /arnt pasb domain protein-protein interaction
Structure deposition date
2012-09-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
96
Peptide accession
Q16665
Residue number A
255
Residue number B
337
Peptide name
Hypoxia-inducible factor 1-alpha

Ligandability

Cysteine 255 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.

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 337 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.

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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