PHD finger protein 23
Intramolecular
Cysteine 356 and cysteine 384
Cysteine 356 and cysteine 381
Cysteine 356 and cysteine 359
Cysteine 381 and cysteine 384
Cysteine 359 and cysteine 381
Cysteine 344 and cysteine 367
Cysteine 359 and cysteine 384
Cysteine 342 and cysteine 367
Cysteine 342 and cysteine 344
Cysteine 342 and cysteine 381
6wxk C 356 C 384
A redox-regulated disulphide may form within PHD finger protein 23 between cysteines 356 and 384.
Details
Redox score ?
91
PDB code
6wxk
Structure name
phf23 phd domain apo
Structure deposition date
2020-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
7
Peptide accession
Q9BUL5
Residue number A
356
Residue number B
384
Peptide name
PHD finger protein 23
Ligandability
Cysteine 356 of PHD finger protein 23
Cysteine 384 of PHD finger protein 23
6wxk D 356 D 381
A redox-regulated disulphide may form within PHD finger protein 23 between cysteines 356 and 381.
Details
Redox score ?
90
PDB code
6wxk
Structure name
phf23 phd domain apo
Structure deposition date
2020-05-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
nan
Peptide accession
Q9BUL5
Residue number A
356
Residue number B
381
Peptide name
PHD finger protein 23
Ligandability
Cysteine 356 of PHD finger protein 23
Cysteine 381 of PHD finger protein 23
6wxk D 356 D 359
A redox-regulated disulphide may form within PHD finger protein 23 between cysteines 356 and 359.
Details
Redox score ?
87
PDB code
6wxk
Structure name
phf23 phd domain apo
Structure deposition date
2020-05-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
nan
Peptide accession
Q9BUL5
Residue number A
356
Residue number B
359
Peptide name
PHD finger protein 23
Ligandability
Cysteine 356 of PHD finger protein 23
Cysteine 359 of PHD finger protein 23
6wxk C 381 C 384
A redox-regulated disulphide may form within PHD finger protein 23 between cysteines 381 and 384.
Details
Redox score ?
86
PDB code
6wxk
Structure name
phf23 phd domain apo
Structure deposition date
2020-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
8
% buried
6
Peptide accession
Q9BUL5
Residue number A
381
Residue number B
384
Peptide name
PHD finger protein 23
Ligandability
Cysteine 381 of PHD finger protein 23
Cysteine 384 of PHD finger protein 23
6wxk C 359 C 381
A redox-regulated disulphide may form within PHD finger protein 23 between cysteines 359 and 381.
Details
Redox score ?
83
PDB code
6wxk
Structure name
phf23 phd domain apo
Structure deposition date
2020-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
16
Peptide accession
Q9BUL5
Residue number A
359
Residue number B
381
Peptide name
PHD finger protein 23
Ligandability
Cysteine 359 of PHD finger protein 23
Cysteine 381 of PHD finger protein 23
6wxk C 344 C 367
A redox-regulated disulphide may form within PHD finger protein 23 between cysteines 344 and 367.
Details
Redox score ?
81
PDB code
6wxk
Structure name
phf23 phd domain apo
Structure deposition date
2020-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
28
Peptide accession
Q9BUL5
Residue number A
344
Residue number B
367
Peptide name
PHD finger protein 23
Ligandability
Cysteine 344 of PHD finger protein 23
Cysteine 367 of PHD finger protein 23
6wxk C 359 C 384
A redox-regulated disulphide may form within PHD finger protein 23 between cysteines 359 and 384.
Details
Redox score ?
80
PDB code
6wxk
Structure name
phf23 phd domain apo
Structure deposition date
2020-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
10
% buried
10
Peptide accession
Q9BUL5
Residue number A
359
Residue number B
384
Peptide name
PHD finger protein 23
Ligandability
Cysteine 359 of PHD finger protein 23
Cysteine 384 of PHD finger protein 23
6wxk C 342 C 367
A redox-regulated disulphide may form within PHD finger protein 23 between cysteines 342 and 367.
Details
Redox score ?
77
PDB code
6wxk
Structure name
phf23 phd domain apo
Structure deposition date
2020-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
32
Peptide accession
Q9BUL5
Residue number A
342
Residue number B
367
Peptide name
PHD finger protein 23
Ligandability
Cysteine 342 of PHD finger protein 23
Cysteine 367 of PHD finger protein 23
6wxk D 342 D 344
A redox-regulated disulphide may form within PHD finger protein 23 between cysteines 342 and 344.
Details
Redox score ?
74
PDB code
6wxk
Structure name
phf23 phd domain apo
Structure deposition date
2020-05-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
33
Peptide accession
Q9BUL5
Residue number A
342
Residue number B
344
Peptide name
PHD finger protein 23
Ligandability
Cysteine 342 of PHD finger protein 23
Cysteine 344 of PHD finger protein 23
6wxk C 342 C 381
A redox-regulated disulphide may form within PHD finger protein 23 between cysteines 342 and 381. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
6wxk
Structure name
phf23 phd domain apo
Structure deposition date
2020-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
29
Peptide accession
Q9BUL5
Residue number A
342
Residue number B
381
Peptide name
PHD finger protein 23
Ligandability
Cysteine 342 of PHD finger protein 23
Cysteine 381 of PHD finger protein 23
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