Protein PML
Intermolecular
Cysteine 66 and cysteine 66
Cysteine 91 and cysteine 91
Cysteine 72 and cysteine 72
Intramolecular
Cysteine 129 and cysteine 151
Cysteine 57 and cysteine 80
Cysteine 60 and cysteine 80
Cysteine 129 and cysteine 148
Cysteine 129 and cysteine 132
Cysteine 72 and cysteine 91
Cysteine 77 and cysteine 80
More...Cysteine 88 and cysteine 91
Cysteine 148 and cysteine 151
Cysteine 57 and cysteine 60
Cysteine 132 and cysteine 151
Cysteine 60 and cysteine 77
Cysteine 72 and cysteine 88
Cysteine 140 and cysteine 143
Cysteine 57 and cysteine 77
Cysteine 132 and cysteine 148
Cysteine 66 and cysteine 91
Cysteine 66 and cysteine 77
Cysteine 66 and cysteine 72
Cysteine 66 and cysteine 80
Cysteine 129 and cysteine 140
Cysteine 66 and cysteine 88
Cysteine 57 and cysteine 66
Cysteine 140 and cysteine 151
5yuf C 66 D 66
A redox-regulated disulphide may form between two units of Protein PML at cysteines 66 and 66.
Details
Redox score ?
80
PDB code
5yuf
Structure name
crystal structure of pml ring tetramer
Structure deposition date
2017-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide A name
Protein PML
Peptide B name
Protein PML
Peptide A accession
P29590
Peptide B accession
P29590
Peptide A residue number
66
Peptide B residue number
66
Ligandability
5yuf B 91 C 91
A redox-regulated disulphide may form between two units of Protein PML at cysteines 91 and 91.
Details
Redox score ?
66
PDB code
5yuf
Structure name
crystal structure of pml ring tetramer
Structure deposition date
2017-11-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
42
Peptide A name
Protein PML
Peptide B name
Protein PML
Peptide A accession
P29590
Peptide B accession
P29590
Peptide A residue number
91
Peptide B residue number
91
Ligandability
5yuf B 72 C 72
A redox-regulated disulphide may form between two units of Protein PML at cysteines 72 and 72. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
5yuf
Structure name
crystal structure of pml ring tetramer
Structure deposition date
2017-11-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
15
% buried
56
Peptide A name
Protein PML
Peptide B name
Protein PML
Peptide A accession
P29590
Peptide B accession
P29590
Peptide A residue number
72
Peptide B residue number
72
Ligandability
6imq A 129 A 151
A redox-regulated disulphide may form within Protein PML between cysteines 129 and 151.
Details
Redox score ?
85
PDB code
6imq
Structure name
crystal structure of pml b1-box multimers
Structure deposition date
2018-10-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
22
Peptide accession
P29590
Residue number A
129
Residue number B
151
Peptide name
Protein PML
Ligandability
Cysteine 129 of Protein PML
Cysteine 151 of Protein PML
1bor A 9 A 32
A redox-regulated disulphide may form within Protein PML between cysteines 57 and 80 (9 and 32 respectively in this structure).
Details
Redox score ?
84
PDB code
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
1
Peptide accession
P29590
Residue number A
57
Residue number B
80
Peptide name
Protein PML
Ligandability
Cysteine 57 of Protein PML
Cysteine 80 of Protein PML
1bor A 12 A 32
A redox-regulated disulphide may form within Protein PML between cysteines 60 and 80 (12 and 32 respectively in this structure).
Details
Redox score ?
84
PDB code
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
0
Peptide accession
P29590
Residue number A
60
Residue number B
80
Peptide name
Protein PML
Ligandability
Cysteine 60 of Protein PML
Cysteine 80 of Protein PML
6imq D 129 D 148
A redox-regulated disulphide may form within Protein PML between cysteines 129 and 148.
Details
Redox score ?
83
PDB code
6imq
Structure name
crystal structure of pml b1-box multimers
Structure deposition date
2018-10-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
2
Peptide accession
P29590
Residue number A
129
Residue number B
148
Peptide name
Protein PML
Ligandability
Cysteine 129 of Protein PML
Cysteine 148 of Protein PML
6imq A 129 A 132
A redox-regulated disulphide may form within Protein PML between cysteines 129 and 132.
Details
Redox score ?
83
PDB code
6imq
Structure name
crystal structure of pml b1-box multimers
Structure deposition date
2018-10-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
17
Peptide accession
P29590
Residue number A
129
Residue number B
132
Peptide name
Protein PML
Ligandability
Cysteine 129 of Protein PML
Cysteine 132 of Protein PML
2mwx A 72 A 91
A redox-regulated disulphide may form within Protein PML between cysteines 72 and 91.
Details
Redox score ?
83
PDB code
2mwx
Structure name
the ring domain of human promyelocytic leukemia protein (pml)
Structure deposition date
2014-12-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
8
% buried
0
Peptide accession
P29590
Residue number A
72
Residue number B
91
Peptide name
Protein PML
Ligandability
Cysteine 72 of Protein PML
Cysteine 91 of Protein PML
1bor A 29 A 32
A redox-regulated disulphide may form within Protein PML between cysteines 77 and 80 (29 and 32 respectively in this structure).
Details
Redox score ?
82
PDB code
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
4
Peptide accession
P29590
Residue number A
77
Residue number B
80
Peptide name
Protein PML
Ligandability
Cysteine 77 of Protein PML
Cysteine 80 of Protein PML
2mwx A 88 A 91
A redox-regulated disulphide may form within Protein PML between cysteines 88 and 91.
Details
Redox score ?
81
PDB code
2mwx
Structure name
the ring domain of human promyelocytic leukemia protein (pml)
Structure deposition date
2014-12-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
0
Peptide accession
P29590
Residue number A
88
Residue number B
91
Peptide name
Protein PML
Ligandability
Cysteine 88 of Protein PML
Cysteine 91 of Protein PML
6imq A 148 A 151
A redox-regulated disulphide may form within Protein PML between cysteines 148 and 151.
Details
Redox score ?
80
PDB code
6imq
Structure name
crystal structure of pml b1-box multimers
Structure deposition date
2018-10-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
6
Peptide accession
P29590
Residue number A
148
Residue number B
151
Peptide name
Protein PML
Ligandability
Cysteine 148 of Protein PML
Cysteine 151 of Protein PML
2mwx A 57 A 60
A redox-regulated disulphide may form within Protein PML between cysteines 57 and 60.
Details
Redox score ?
80
PDB code
2mwx
Structure name
the ring domain of human promyelocytic leukemia protein (pml)
Structure deposition date
2014-12-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
9
Peptide accession
P29590
Residue number A
57
Residue number B
60
Peptide name
Protein PML
Ligandability
Cysteine 57 of Protein PML
Cysteine 60 of Protein PML
6imq D 132 D 151
A redox-regulated disulphide may form within Protein PML between cysteines 132 and 151.
Details
Redox score ?
80
PDB code
6imq
Structure name
crystal structure of pml b1-box multimers
Structure deposition date
2018-10-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
P29590
Residue number A
132
Residue number B
151
Peptide name
Protein PML
Ligandability
Cysteine 132 of Protein PML
Cysteine 151 of Protein PML
1bor A 12 A 29
A redox-regulated disulphide may form within Protein PML between cysteines 60 and 77 (12 and 29 respectively in this structure).
Details
Redox score ?
78
PDB code
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
4
Peptide accession
P29590
Residue number A
60
Residue number B
77
Peptide name
Protein PML
Ligandability
Cysteine 60 of Protein PML
Cysteine 77 of Protein PML
1bor A 24 A 40
A redox-regulated disulphide may form within Protein PML between cysteines 72 and 88 (24 and 40 respectively in this structure).
Details
Redox score ?
77
PDB code
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
22
Peptide accession
P29590
Residue number A
72
Residue number B
88
Peptide name
Protein PML
Ligandability
Cysteine 72 of Protein PML
Cysteine 88 of Protein PML
6imq D 140 D 143
A redox-regulated disulphide may form within Protein PML between cysteines 140 and 143.
Details
Redox score ?
76
PDB code
6imq
Structure name
crystal structure of pml b1-box multimers
Structure deposition date
2018-10-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
26
Peptide accession
P29590
Residue number A
140
Residue number B
143
Peptide name
Protein PML
Ligandability
Cysteine 140 of Protein PML
Cysteine 143 of Protein PML
1bor A 9 A 29
A redox-regulated disulphide may form within Protein PML between cysteines 57 and 77 (9 and 29 respectively in this structure).
Details
Redox score ?
74
PDB code
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
4
Peptide accession
P29590
Residue number A
57
Residue number B
77
Peptide name
Protein PML
Ligandability
Cysteine 57 of Protein PML
Cysteine 77 of Protein PML
6imq D 132 D 148
A redox-regulated disulphide may form within Protein PML between cysteines 132 and 148.
Details
Redox score ?
74
PDB code
6imq
Structure name
crystal structure of pml b1-box multimers
Structure deposition date
2018-10-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
0
Peptide accession
P29590
Residue number A
132
Residue number B
148
Peptide name
Protein PML
Ligandability
Cysteine 132 of Protein PML
Cysteine 148 of Protein PML
1bor A 18 A 43
A redox-regulated disulphide may form within Protein PML between cysteines 66 and 91 (18 and 43 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
26
Peptide accession
P29590
Residue number A
66
Residue number B
91
Peptide name
Protein PML
Ligandability
Cysteine 66 of Protein PML
Cysteine 91 of Protein PML
1bor A 18 A 29
A redox-regulated disulphide may form within Protein PML between cysteines 66 and 77 (18 and 29 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
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
23
Peptide accession
P29590
Residue number A
66
Residue number B
77
Peptide name
Protein PML
Ligandability
Cysteine 66 of Protein PML
Cysteine 77 of Protein PML
1bor A 18 A 24
A redox-regulated disulphide may form within Protein PML between cysteines 66 and 72 (18 and 24 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
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
32
Peptide accession
P29590
Residue number A
66
Residue number B
72
Peptide name
Protein PML
Ligandability
Cysteine 66 of Protein PML
Cysteine 72 of Protein PML
1bor A 18 A 32
A redox-regulated disulphide may form within Protein PML between cysteines 66 and 80 (18 and 32 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
20
Peptide accession
P29590
Residue number A
66
Residue number B
80
Peptide name
Protein PML
Ligandability
Cysteine 66 of Protein PML
Cysteine 80 of Protein PML
2mvw B 129 B 140
A redox-regulated disulphide may form within Protein PML between cysteines 129 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
2mvw
Structure name
solution structure of the trim19 b-box1 (b1) of human promyelocytic leukemia (pml)
Structure deposition date
2014-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
20
Peptide accession
P29590
Residue number A
129
Residue number B
140
Peptide name
Protein PML
Ligandability
Cysteine 129 of Protein PML
Cysteine 140 of Protein PML
1bor A 18 A 40
A redox-regulated disulphide may form within Protein PML between cysteines 66 and 88 (18 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
30
Peptide accession
P29590
Residue number A
66
Residue number B
88
Peptide name
Protein PML
Ligandability
Cysteine 66 of Protein PML
Cysteine 88 of Protein PML
1bor A 9 A 18
A redox-regulated disulphide may form within Protein PML between cysteines 57 and 66 (9 and 18 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
1bor
Structure name
transcription factor pml, a proto-oncoprotein, nmr, 1 representative structure at ph 7
Structure deposition date
1995-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
20
Peptide accession
P29590
Residue number A
57
Residue number B
66
Peptide name
Protein PML
Ligandability
Cysteine 57 of Protein PML
Cysteine 66 of Protein PML
2mvw A 140 A 151
A redox-regulated disulphide may form within Protein PML between cysteines 140 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
2mvw
Structure name
solution structure of the trim19 b-box1 (b1) of human promyelocytic leukemia (pml)
Structure deposition date
2014-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
20
Peptide accession
P29590
Residue number A
140
Residue number B
151
Peptide name
Protein PML
Ligandability
Cysteine 140 of Protein PML
Cysteine 151 of Protein PML
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