ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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PHD finger protein 21A

Intramolecular
Cysteine 503 and cysteine 532
Cysteine 491 and cysteine 494
Cysteine 491 and cysteine 514
Cysteine 503 and cysteine 529
Cysteine 503 and cysteine 506
Cysteine 494 and cysteine 514
Cysteine 506 and cysteine 529
Cysteine 529 and cysteine 532
Cysteine 506 and cysteine 532
A redox-regulated disulphide may form within PHD finger protein 21A between cysteines 503 and 532.

Details

Redox score ?
90
PDB code
2puy
Structure name
crystal structure of the bhc80 phd finger
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
3
% buried
44
Peptide accession
Q96BD5
Residue number A
503
Residue number B
532
Peptide name
PHD finger protein 21A

Ligandability

Cysteine 503 of PHD finger protein 21A

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 532 of PHD finger protein 21A

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 PHD finger protein 21A between cysteines 491 and 494.

Details

Redox score ?
86
PDB code
2puy
Structure name
crystal structure of the bhc80 phd finger
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
4
Peptide accession
Q96BD5
Residue number A
491
Residue number B
494
Peptide name
PHD finger protein 21A

Ligandability

Cysteine 491 of PHD finger protein 21A

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 494 of PHD finger protein 21A

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 PHD finger protein 21A between cysteines 491 and 514.

Details

Redox score ?
86
PDB code
2puy
Structure name
crystal structure of the bhc80 phd finger
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
5
% buried
16
Peptide accession
Q96BD5
Residue number A
491
Residue number B
514
Peptide name
PHD finger protein 21A

Ligandability

Cysteine 491 of PHD finger protein 21A

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 514 of PHD finger protein 21A

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 PHD finger protein 21A between cysteines 503 and 529.

Details

Redox score ?
84
PDB code
2puy
Structure name
crystal structure of the bhc80 phd finger
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
5
% buried
38
Peptide accession
Q96BD5
Residue number A
503
Residue number B
529
Peptide name
PHD finger protein 21A

Ligandability

Cysteine 503 of PHD finger protein 21A

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 529 of PHD finger protein 21A

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 PHD finger protein 21A between cysteines 503 and 506.

Details

Redox score ?
84
PDB code
2puy
Structure name
crystal structure of the bhc80 phd finger
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
24
Peptide accession
Q96BD5
Residue number A
503
Residue number B
506
Peptide name
PHD finger protein 21A

Ligandability

Cysteine 503 of PHD finger protein 21A

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 PHD finger protein 21A

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 PHD finger protein 21A between cysteines 494 and 514.

Details

Redox score ?
81
PDB code
2puy
Structure name
crystal structure of the bhc80 phd finger
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
0
Peptide accession
Q96BD5
Residue number A
494
Residue number B
514
Peptide name
PHD finger protein 21A

Ligandability

Cysteine 494 of PHD finger protein 21A

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 514 of PHD finger protein 21A

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 PHD finger protein 21A between cysteines 506 and 529.

Details

Redox score ?
78
PDB code
2puy
Structure name
crystal structure of the bhc80 phd finger
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
31
Peptide accession
Q96BD5
Residue number A
506
Residue number B
529
Peptide name
PHD finger protein 21A

Ligandability

Cysteine 506 of PHD finger protein 21A

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 529 of PHD finger protein 21A

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 PHD finger protein 21A between cysteines 529 and 532.

Details

Redox score ?
75
PDB code
2puy
Structure name
crystal structure of the bhc80 phd finger
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
43
Peptide accession
Q96BD5
Residue number A
529
Residue number B
532
Peptide name
PHD finger protein 21A

Ligandability

Cysteine 529 of PHD finger protein 21A

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 532 of PHD finger protein 21A

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 PHD finger protein 21A between cysteines 506 and 532.

Details

Redox score ?
75
PDB code
2puy
Structure name
crystal structure of the bhc80 phd finger
Structure deposition date
2007-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
11
% buried
20
Peptide accession
Q96BD5
Residue number A
506
Residue number B
532
Peptide name
PHD finger protein 21A

Ligandability

Cysteine 506 of PHD finger protein 21A

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 532 of PHD finger protein 21A

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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