PHD finger protein 20
Intramolecular
Cysteine 669 and cysteine 672
Cysteine 672 and cysteine 697
Cysteine 672 and cysteine 694
Cysteine 655 and cysteine 657
Cysteine 655 and cysteine 680
Cysteine 694 and cysteine 697
Cysteine 669 and cysteine 694
Cysteine 669 and cysteine 697
Cysteine 672 and cysteine 674
Cysteine 657 and cysteine 680
More...Cysteine 674 and cysteine 694
Cysteine 669 and cysteine 674
Cysteine 96 and cysteine 100
Cysteine 674 and cysteine 697
Cysteine 655 and cysteine 694
Cysteine 655 and cysteine 674
5tab A 24 A 27
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 669 and 672 (24 and 27 respectively in this structure).
Details
Redox score ?
88
PDB code
5tab
Structure name
crystal structure of the phd finger of phf20
Structure deposition date
2016-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
8
Peptide accession
Q9BVI0
Residue number A
669
Residue number B
672
Peptide name
PHD finger protein 20
Ligandability
Cysteine 669 of PHD finger protein 20
Cysteine 672 of PHD finger protein 20
5tab A 27 A 52
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 672 and 697 (27 and 52 respectively in this structure).
Details
Redox score ?
88
PDB code
5tab
Structure name
crystal structure of the phd finger of phf20
Structure deposition date
2016-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
5
% buried
4
Peptide accession
Q9BVI0
Residue number A
672
Residue number B
697
Peptide name
PHD finger protein 20
Ligandability
Cysteine 672 of PHD finger protein 20
Cysteine 697 of PHD finger protein 20
5tab A 27 A 49
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 672 and 694 (27 and 49 respectively in this structure).
Details
Redox score ?
88
PDB code
5tab
Structure name
crystal structure of the phd finger of phf20
Structure deposition date
2016-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
10
Peptide accession
Q9BVI0
Residue number A
672
Residue number B
694
Peptide name
PHD finger protein 20
Ligandability
Cysteine 672 of PHD finger protein 20
Cysteine 694 of PHD finger protein 20
5tab A 10 A 12
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 655 and 657 (10 and 12 respectively in this structure).
Details
Redox score ?
87
PDB code
5tab
Structure name
crystal structure of the phd finger of phf20
Structure deposition date
2016-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
9
Peptide accession
Q9BVI0
Residue number A
655
Residue number B
657
Peptide name
PHD finger protein 20
Ligandability
Cysteine 655 of PHD finger protein 20
Cysteine 657 of PHD finger protein 20
5tab A 10 A 35
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 655 and 680 (10 and 35 respectively in this structure).
Details
Redox score ?
86
PDB code
5tab
Structure name
crystal structure of the phd finger of phf20
Structure deposition date
2016-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
9
Peptide accession
Q9BVI0
Residue number A
655
Residue number B
680
Peptide name
PHD finger protein 20
Ligandability
Cysteine 655 of PHD finger protein 20
Cysteine 680 of PHD finger protein 20
5tab A 49 A 52
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 694 and 697 (49 and 52 respectively in this structure).
Details
Redox score ?
85
PDB code
5tab
Structure name
crystal structure of the phd finger of phf20
Structure deposition date
2016-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
6
Peptide accession
Q9BVI0
Residue number A
694
Residue number B
697
Peptide name
PHD finger protein 20
Ligandability
Cysteine 694 of PHD finger protein 20
Cysteine 697 of PHD finger protein 20
5tab A 24 A 49
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 669 and 694 (24 and 49 respectively in this structure).
Details
Redox score ?
84
PDB code
5tab
Structure name
crystal structure of the phd finger of phf20
Structure deposition date
2016-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
9
Peptide accession
Q9BVI0
Residue number A
669
Residue number B
694
Peptide name
PHD finger protein 20
Ligandability
Cysteine 669 of PHD finger protein 20
Cysteine 694 of PHD finger protein 20
5tab A 24 A 52
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 669 and 697 (24 and 52 respectively in this structure).
Details
Redox score ?
84
PDB code
5tab
Structure name
crystal structure of the phd finger of phf20
Structure deposition date
2016-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
3
Peptide accession
Q9BVI0
Residue number A
669
Residue number B
697
Peptide name
PHD finger protein 20
Ligandability
Cysteine 669 of PHD finger protein 20
Cysteine 697 of PHD finger protein 20
5tbn A 26 A 28
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 672 and 674 (26 and 28 respectively in this structure).
Details
Redox score ?
81
PDB code
5tbn
Structure name
solution nmr structure of phf20 phd domain in complex with a histone h3k4me2 peptide
Structure deposition date
2016-09-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
35
Peptide accession
Q9BVI0
Residue number A
672
Residue number B
674
Peptide name
PHD finger protein 20
Ligandability
Cysteine 672 of PHD finger protein 20
Cysteine 674 of PHD finger protein 20
5tab A 12 A 35
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 657 and 680 (12 and 35 respectively in this structure).
Details
Redox score ?
80
PDB code
5tab
Structure name
crystal structure of the phd finger of phf20
Structure deposition date
2016-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
0
Peptide accession
Q9BVI0
Residue number A
657
Residue number B
680
Peptide name
PHD finger protein 20
Ligandability
Cysteine 657 of PHD finger protein 20
Cysteine 680 of PHD finger protein 20
5tbn A 28 A 48
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 674 and 694 (28 and 48 respectively in this structure).
Details
Redox score ?
79
PDB code
5tbn
Structure name
solution nmr structure of phf20 phd domain in complex with a histone h3k4me2 peptide
Structure deposition date
2016-09-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
36
Peptide accession
Q9BVI0
Residue number A
674
Residue number B
694
Peptide name
PHD finger protein 20
Ligandability
Cysteine 674 of PHD finger protein 20
Cysteine 694 of PHD finger protein 20
5tbn A 23 A 28
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 669 and 674 (23 and 28 respectively in this structure).
Details
Redox score ?
77
PDB code
5tbn
Structure name
solution nmr structure of phf20 phd domain in complex with a histone h3k4me2 peptide
Structure deposition date
2016-09-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
34
Peptide accession
Q9BVI0
Residue number A
669
Residue number B
674
Peptide name
PHD finger protein 20
Ligandability
Cysteine 669 of PHD finger protein 20
Cysteine 674 of PHD finger protein 20
3qii A 96 A 100
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 96 and 100.
Details
Redox score ?
69
PDB code
3qii
Structure name
crystal structure of tudor domain 2 of human phd finger protein 20
Structure deposition date
2011-01-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BVI0
Residue number A
96
Residue number B
100
Peptide name
PHD finger protein 20
Ligandability
Cysteine 96 of PHD finger protein 20
Cysteine 100 of PHD finger protein 20
5tbn A 28 A 51
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 674 and 697 (28 and 51 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
5tbn
Structure name
solution nmr structure of phf20 phd domain in complex with a histone h3k4me2 peptide
Structure deposition date
2016-09-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
48
Minimum pKa ?
12
% buried
22
Peptide accession
Q9BVI0
Residue number A
674
Residue number B
697
Peptide name
PHD finger protein 20
Ligandability
Cysteine 674 of PHD finger protein 20
Cysteine 697 of PHD finger protein 20
5tab A 10 A 49
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 655 and 694 (10 and 49 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
5tab
Structure name
crystal structure of the phd finger of phf20
Structure deposition date
2016-09-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
15
Peptide accession
Q9BVI0
Residue number A
655
Residue number B
694
Peptide name
PHD finger protein 20
Ligandability
Cysteine 655 of PHD finger protein 20
Cysteine 694 of PHD finger protein 20
5tbn A 9 A 28
A redox-regulated disulphide may form within PHD finger protein 20 between cysteines 655 and 674 (9 and 28 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
5tbn
Structure name
solution nmr structure of phf20 phd domain in complex with a histone h3k4me2 peptide
Structure deposition date
2016-09-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
32
Peptide accession
Q9BVI0
Residue number A
655
Residue number B
674
Peptide name
PHD finger protein 20
Ligandability
Cysteine 655 of PHD finger protein 20
Cysteine 674 of PHD finger protein 20
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