PHD finger protein 1
Intramolecular
Cysteine 204 and cysteine 234
Cysteine 110 and cysteine 136
Cysteine 90 and cysteine 93
Cysteine 93 and cysteine 118
Cysteine 107 and cysteine 110
Cysteine 107 and cysteine 139
Cysteine 107 and cysteine 136
Cysteine 189 and cysteine 191
Cysteine 207 and cysteine 237
Cysteine 234 and cysteine 237
More...Cysteine 204 and cysteine 237
Cysteine 265 and cysteine 266
Cysteine 91 and cysteine 110
Cysteine 189 and cysteine 215
Cysteine 204 and cysteine 207
Cysteine 90 and cysteine 91
Cysteine 207 and cysteine 234
Cysteine 136 and cysteine 139
Cysteine 110 and cysteine 139
Cysteine 204 and cysteine 235
Cysteine 91 and cysteine 136
Cysteine 90 and cysteine 118
Cysteine 234 and cysteine 235
Cysteine 91 and cysteine 107
Cysteine 191 and cysteine 215
Cysteine 91 and cysteine 93
Cysteine 91 and cysteine 118
Cysteine 218 and cysteine 235
Cysteine 189 and cysteine 235
Cysteine 189 and cysteine 234
Cysteine 235 and cysteine 237
Cysteine 91 and cysteine 139
5xfq B 204 B 234
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 204 and 234.
Details
Redox score ?
93
PDB code
5xfq
Structure name
ternary complex of phf1, a dna duplex and a histone peptide
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
0
% buried
57
Peptide accession
Q9Z1B8
Residue number A
204
Residue number B
234
Peptide name
PHD finger protein 1
Ligandability
Cysteine 204 of PHD finger protein 1
Cysteine 234 of PHD finger protein 1
5xfp B 110 B 136
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 110 and 136.
Details
Redox score ?
91
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
1
% buried
66
Peptide accession
O43189
Residue number A
110
Residue number B
136
Peptide name
PHD finger protein 1
Ligandability
Cysteine 110 of PHD finger protein 1
Cysteine 136 of PHD finger protein 1
5xfp A 90 A 93
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 90 and 93.
Details
Redox score ?
85
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
16
Peptide accession
O43189
Residue number A
90
Residue number B
93
Peptide name
PHD finger protein 1
Ligandability
Cysteine 90 of PHD finger protein 1
Cysteine 93 of PHD finger protein 1
5xfp E 93 E 118
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 93 and 118.
Details
Redox score ?
81
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
6
Peptide accession
O43189
Residue number A
93
Residue number B
118
Peptide name
PHD finger protein 1
Ligandability
Cysteine 93 of PHD finger protein 1
Cysteine 118 of PHD finger protein 1
5xfn A 107 A 110
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 107 and 110.
Details
Redox score ?
80
PDB code
5xfn
Structure name
structure of the n-terminal domains of phf1
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
48
Peptide accession
O43189
Residue number A
107
Residue number B
110
Peptide name
PHD finger protein 1
Ligandability
Cysteine 107 of PHD finger protein 1
Cysteine 110 of PHD finger protein 1
5xfp A 107 A 139
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 107 and 139.
Details
Redox score ?
80
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
42
Peptide accession
O43189
Residue number A
107
Residue number B
139
Peptide name
PHD finger protein 1
Ligandability
Cysteine 107 of PHD finger protein 1
Cysteine 139 of PHD finger protein 1
5xfp A 107 A 136
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 107 and 136.
Details
Redox score ?
78
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
56
Peptide accession
O43189
Residue number A
107
Residue number B
136
Peptide name
PHD finger protein 1
Ligandability
Cysteine 107 of PHD finger protein 1
Cysteine 136 of PHD finger protein 1
5xfq B 189 B 191
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 189 and 191.
Details
Redox score ?
76
PDB code
5xfq
Structure name
ternary complex of phf1, a dna duplex and a histone peptide
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
91
Minimum pKa ?
6
% buried
nan
Peptide accession
Q9Z1B8
Residue number A
189
Residue number B
191
Peptide name
PHD finger protein 1
Ligandability
Cysteine 189 of PHD finger protein 1
Cysteine 191 of PHD finger protein 1
5xfp B 207 B 237
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 207 and 237.
Details
Redox score ?
75
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
44
Peptide accession
O43189
Residue number A
207
Residue number B
237
Peptide name
PHD finger protein 1
Ligandability
Cysteine 207 of PHD finger protein 1
Cysteine 237 of PHD finger protein 1
5xfq B 234 B 237
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 234 and 237.
Details
Redox score ?
75
PDB code
5xfq
Structure name
ternary complex of phf1, a dna duplex and a histone peptide
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
42
Peptide accession
Q9Z1B8
Residue number A
234
Residue number B
237
Peptide name
PHD finger protein 1
Ligandability
Cysteine 234 of PHD finger protein 1
Cysteine 237 of PHD finger protein 1
5xfn A 204 A 237
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 204 and 237.
Details
Redox score ?
74
PDB code
5xfn
Structure name
structure of the n-terminal domains of phf1
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
nan
Peptide accession
O43189
Residue number A
204
Residue number B
237
Peptide name
PHD finger protein 1
Ligandability
Cysteine 204 of PHD finger protein 1
Cysteine 237 of PHD finger protein 1
5xfq A 265 A 266
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 265 and 266.
Details
Redox score ?
74
PDB code
5xfq
Structure name
ternary complex of phf1, a dna duplex and a histone peptide
Structure deposition date
2017-04-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
36
Minimum pKa ?
9
% buried
16
Peptide accession
Q9Z1B8
Residue number A
265
Residue number B
266
Peptide name
PHD finger protein 1
Ligandability
Cysteine 265 of PHD finger protein 1
Cysteine 266 of PHD finger protein 1
5xfp B 91 B 110
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 91 and 110.
Details
Redox score ?
74
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
1
% buried
59
Peptide accession
O43189
Residue number A
91
Residue number B
110
Peptide name
PHD finger protein 1
Ligandability
Cysteine 91 of PHD finger protein 1
Cysteine 110 of PHD finger protein 1
5xfo A 189 A 215
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 189 and 215.
Details
Redox score ?
74
PDB code
5xfo
Structure name
structure of the n-terminal domains of phf1
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
6
% buried
100
Peptide accession
O43189
Residue number A
189
Residue number B
215
Peptide name
PHD finger protein 1
Ligandability
Cysteine 189 of PHD finger protein 1
Cysteine 215 of PHD finger protein 1
5xfq A 204 A 207
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 204 and 207.
Details
Redox score ?
73
PDB code
5xfq
Structure name
ternary complex of phf1, a dna duplex and a histone peptide
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9Z1B8
Residue number A
204
Residue number B
207
Peptide name
PHD finger protein 1
Ligandability
Cysteine 204 of PHD finger protein 1
Cysteine 207 of PHD finger protein 1
5xfp E 90 E 91
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 90 and 91.
Details
Redox score ?
71
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
46
Peptide accession
O43189
Residue number A
90
Residue number B
91
Peptide name
PHD finger protein 1
Ligandability
Cysteine 90 of PHD finger protein 1
Cysteine 91 of PHD finger protein 1
5xfn A 207 A 234
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 207 and 234.
Details
Redox score ?
69
PDB code
5xfn
Structure name
structure of the n-terminal domains of phf1
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
63
Peptide accession
O43189
Residue number A
207
Residue number B
234
Peptide name
PHD finger protein 1
Ligandability
Cysteine 207 of PHD finger protein 1
Cysteine 234 of PHD finger protein 1
5xfo A 136 A 139
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 136 and 139.
Details
Redox score ?
63
PDB code
5xfo
Structure name
structure of the n-terminal domains of phf1
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
13
% buried
60
Peptide accession
O43189
Residue number A
136
Residue number B
139
Peptide name
PHD finger protein 1
Ligandability
Cysteine 136 of PHD finger protein 1
Cysteine 139 of PHD finger protein 1
5xfq A 110 A 139
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 110 and 139.
Details
Redox score ?
62
PDB code
5xfq
Structure name
ternary complex of phf1, a dna duplex and a histone peptide
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
14
% buried
69
Peptide accession
Q9Z1B8
Residue number A
110
Residue number B
139
Peptide name
PHD finger protein 1
Ligandability
Cysteine 110 of PHD finger protein 1
Cysteine 139 of PHD finger protein 1
5xfq B 204 B 235
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 204 and 235.
Details
Redox score ?
60
PDB code
5xfq
Structure name
ternary complex of phf1, a dna duplex and a histone peptide
Structure deposition date
2017-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
0
% buried
56
Peptide accession
Q9Z1B8
Residue number A
204
Residue number B
235
Peptide name
PHD finger protein 1
Ligandability
Cysteine 204 of PHD finger protein 1
Cysteine 235 of PHD finger protein 1
5xfp A 91 A 136
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 91 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
70
Peptide accession
O43189
Residue number A
91
Residue number B
136
Peptide name
PHD finger protein 1
Ligandability
Cysteine 91 of PHD finger protein 1
Cysteine 136 of PHD finger protein 1
5xfq A 90 A 118
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 90 and 118. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5xfq
Structure name
ternary complex of phf1, a dna duplex and a histone peptide
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
18
% buried
nan
Peptide accession
Q9Z1B8
Residue number A
90
Residue number B
118
Peptide name
PHD finger protein 1
Ligandability
Cysteine 90 of PHD finger protein 1
Cysteine 118 of PHD finger protein 1
5xfp A 234 A 235
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 234 and 235. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
62
Peptide accession
O43189
Residue number A
234
Residue number B
235
Peptide name
PHD finger protein 1
Ligandability
Cysteine 234 of PHD finger protein 1
Cysteine 235 of PHD finger protein 1
5xfn A 91 A 107
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 91 and 107. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5xfn
Structure name
structure of the n-terminal domains of phf1
Structure deposition date
2017-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
55
Peptide accession
O43189
Residue number A
91
Residue number B
107
Peptide name
PHD finger protein 1
Ligandability
Cysteine 91 of PHD finger protein 1
Cysteine 107 of PHD finger protein 1
5xfn A 191 A 215
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 191 and 215. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5xfn
Structure name
structure of the n-terminal domains of phf1
Structure deposition date
2017-04-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
91
Minimum pKa ?
19
% buried
nan
Peptide accession
O43189
Residue number A
191
Residue number B
215
Peptide name
PHD finger protein 1
Ligandability
Cysteine 191 of PHD finger protein 1
Cysteine 215 of PHD finger protein 1
5xfq A 91 A 93
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 91 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
5xfq
Structure name
ternary complex of phf1, a dna duplex and a histone peptide
Structure deposition date
2017-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
70
Peptide accession
Q9Z1B8
Residue number A
91
Residue number B
93
Peptide name
PHD finger protein 1
Ligandability
Cysteine 91 of PHD finger protein 1
Cysteine 93 of PHD finger protein 1
5xfn A 91 A 118
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 91 and 118. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5xfn
Structure name
structure of the n-terminal domains of phf1
Structure deposition date
2017-04-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
42
Peptide accession
O43189
Residue number A
91
Residue number B
118
Peptide name
PHD finger protein 1
Ligandability
Cysteine 91 of PHD finger protein 1
Cysteine 118 of PHD finger protein 1
5xfp A 218 A 235
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 218 and 235. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
69
Peptide accession
O43189
Residue number A
218
Residue number B
235
Peptide name
PHD finger protein 1
Ligandability
Cysteine 218 of PHD finger protein 1
Cysteine 235 of PHD finger protein 1
5xfp A 189 A 235
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 189 and 235. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
6
% buried
81
Peptide accession
O43189
Residue number A
189
Residue number B
235
Peptide name
PHD finger protein 1
Ligandability
Cysteine 189 of PHD finger protein 1
Cysteine 235 of PHD finger protein 1
5xfq A 189 A 234
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 189 and 234. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5xfq
Structure name
ternary complex of phf1, a dna duplex and a histone peptide
Structure deposition date
2017-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
9
% buried
82
Peptide accession
Q9Z1B8
Residue number A
189
Residue number B
234
Peptide name
PHD finger protein 1
Ligandability
Cysteine 189 of PHD finger protein 1
Cysteine 234 of PHD finger protein 1
5xfo A 235 A 237
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 235 and 237. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5xfo
Structure name
structure of the n-terminal domains of phf1
Structure deposition date
2017-04-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
11
% buried
45
Peptide accession
O43189
Residue number A
235
Residue number B
237
Peptide name
PHD finger protein 1
Ligandability
Cysteine 235 of PHD finger protein 1
Cysteine 237 of PHD finger protein 1
5xfp B 91 B 139
A redox-regulated disulphide may form within PHD finger protein 1 between cysteines 91 and 139. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
5xfp
Structure name
binary complex of phf1 and a double stranded dna
Structure deposition date
2017-04-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
54
Peptide accession
O43189
Residue number A
91
Residue number B
139
Peptide name
PHD finger protein 1
Ligandability
Cysteine 91 of PHD finger protein 1
Cysteine 139 of PHD finger protein 1
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