RING finger protein 141
Intramolecular
Cysteine 155 and cysteine 158
Cysteine 155 and cysteine 177
Cysteine 155 and cysteine 174
Cysteine 169 and cysteine 188
Cysteine 188 and cysteine 191
Cysteine 174 and cysteine 177
Cysteine 158 and cysteine 174
Cysteine 169 and cysteine 191
Cysteine 158 and cysteine 177
Cysteine 155 and cysteine 156
More...Cysteine 155 and cysteine 188
Cysteine 156 and cysteine 188
Cysteine 156 and cysteine 174
Cysteine 156 and cysteine 191
Cysteine 156 and cysteine 169
Cysteine 177 and cysteine 188
Cysteine 156 and cysteine 158
Cysteine 156 and cysteine 177
5xek A 4 A 7
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 155 and 158 (4 and 7 respectively in this structure).
Details
Redox score ?
88
PDB code
5xek
Structure name
c-terminal zinc finger of ring finger protein 141
Structure deposition date
2017-04-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
5
% buried
0
Peptide accession
Q8WVD5
Residue number A
155
Residue number B
158
Peptide name
RING finger protein 141
Ligandability
Cysteine 155 of RING finger protein 141
Cysteine 158 of RING finger protein 141
5xek A 4 A 26
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 155 and 177 (4 and 26 respectively in this structure).
Details
Redox score ?
88
PDB code
5xek
Structure name
c-terminal zinc finger of ring finger protein 141
Structure deposition date
2017-04-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
0
Peptide accession
Q8WVD5
Residue number A
155
Residue number B
177
Peptide name
RING finger protein 141
Ligandability
Cysteine 155 of RING finger protein 141
Cysteine 177 of RING finger protein 141
2ecn A 18 A 37
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 155 and 174 (18 and 37 respectively in this structure).
Details
Redox score ?
88
PDB code
2ecn
Structure name
solution structure of the ring domain of the human ring finger protein 141
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
1
Peptide accession
Q8WVD5
Residue number A
155
Residue number B
174
Peptide name
RING finger protein 141
Ligandability
Cysteine 155 of RING finger protein 141
Cysteine 174 of RING finger protein 141
2ecn A 32 A 51
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 169 and 188 (32 and 51 respectively in this structure).
Details
Redox score ?
86
PDB code
2ecn
Structure name
solution structure of the ring domain of the human ring finger protein 141
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
1
Peptide accession
Q8WVD5
Residue number A
169
Residue number B
188
Peptide name
RING finger protein 141
Ligandability
Cysteine 169 of RING finger protein 141
Cysteine 188 of RING finger protein 141
2ecn A 51 A 54
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 188 and 191 (51 and 54 respectively in this structure).
Details
Redox score ?
85
PDB code
2ecn
Structure name
solution structure of the ring domain of the human ring finger protein 141
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
1
Peptide accession
Q8WVD5
Residue number A
188
Residue number B
191
Peptide name
RING finger protein 141
Ligandability
Cysteine 188 of RING finger protein 141
Cysteine 191 of RING finger protein 141
2ecn A 37 A 40
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 174 and 177 (37 and 40 respectively in this structure).
Details
Redox score ?
83
PDB code
2ecn
Structure name
solution structure of the ring domain of the human ring finger protein 141
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
0
Peptide accession
Q8WVD5
Residue number A
174
Residue number B
177
Peptide name
RING finger protein 141
Ligandability
Cysteine 174 of RING finger protein 141
Cysteine 177 of RING finger protein 141
2ecn A 21 A 37
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 158 and 174 (21 and 37 respectively in this structure).
Details
Redox score ?
83
PDB code
2ecn
Structure name
solution structure of the ring domain of the human ring finger protein 141
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
Q8WVD5
Residue number A
158
Residue number B
174
Peptide name
RING finger protein 141
Ligandability
Cysteine 158 of RING finger protein 141
Cysteine 174 of RING finger protein 141
5xek A 18 A 40
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 169 and 191 (18 and 40 respectively in this structure).
Details
Redox score ?
82
PDB code
5xek
Structure name
c-terminal zinc finger of ring finger protein 141
Structure deposition date
2017-04-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
31
Minimum pKa ?
9
% buried
0
Peptide accession
Q8WVD5
Residue number A
169
Residue number B
191
Peptide name
RING finger protein 141
Ligandability
Cysteine 169 of RING finger protein 141
Cysteine 191 of RING finger protein 141
5xek A 7 A 26
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 158 and 177 (7 and 26 respectively in this structure).
Details
Redox score ?
77
PDB code
5xek
Structure name
c-terminal zinc finger of ring finger protein 141
Structure deposition date
2017-04-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
10
% buried
0
Peptide accession
Q8WVD5
Residue number A
158
Residue number B
177
Peptide name
RING finger protein 141
Ligandability
Cysteine 158 of RING finger protein 141
Cysteine 177 of RING finger protein 141
5xek A 4 A 5
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 155 and 156 (4 and 5 respectively in this structure).
Details
Redox score ?
70
PDB code
5xek
Structure name
c-terminal zinc finger of ring finger protein 141
Structure deposition date
2017-04-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
0
Peptide accession
Q8WVD5
Residue number A
155
Residue number B
156
Peptide name
RING finger protein 141
Ligandability
Cysteine 155 of RING finger protein 141
Cysteine 156 of RING finger protein 141
5xek A 4 A 37
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 155 and 188 (4 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5xek
Structure name
c-terminal zinc finger of ring finger protein 141
Structure deposition date
2017-04-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
0
Peptide accession
Q8WVD5
Residue number A
155
Residue number B
188
Peptide name
RING finger protein 141
Ligandability
Cysteine 155 of RING finger protein 141
Cysteine 188 of RING finger protein 141
2ecn A 19 A 51
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 156 and 188 (19 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 ?
55
PDB code
2ecn
Structure name
solution structure of the ring domain of the human ring finger protein 141
Structure deposition date
2007-02-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
2
Peptide accession
Q8WVD5
Residue number A
156
Residue number B
188
Peptide name
RING finger protein 141
Ligandability
Cysteine 156 of RING finger protein 141
Cysteine 188 of RING finger protein 141
5xek A 5 A 23
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 156 and 174 (5 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
5xek
Structure name
c-terminal zinc finger of ring finger protein 141
Structure deposition date
2017-04-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
0
Peptide accession
Q8WVD5
Residue number A
156
Residue number B
174
Peptide name
RING finger protein 141
Ligandability
Cysteine 156 of RING finger protein 141
Cysteine 174 of RING finger protein 141
5xek A 5 A 40
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 156 and 191 (5 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 ?
47
PDB code
5xek
Structure name
c-terminal zinc finger of ring finger protein 141
Structure deposition date
2017-04-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
40
Minimum pKa ?
9
% buried
0
Peptide accession
Q8WVD5
Residue number A
156
Residue number B
191
Peptide name
RING finger protein 141
Ligandability
Cysteine 156 of RING finger protein 141
Cysteine 191 of RING finger protein 141
5xek A 5 A 18
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 156 and 169 (5 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 ?
47
PDB code
5xek
Structure name
c-terminal zinc finger of ring finger protein 141
Structure deposition date
2017-04-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
0
Peptide accession
Q8WVD5
Residue number A
156
Residue number B
169
Peptide name
RING finger protein 141
Ligandability
Cysteine 156 of RING finger protein 141
Cysteine 169 of RING finger protein 141
5xek A 26 A 37
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 177 and 188 (26 and 37 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
5xek
Structure name
c-terminal zinc finger of ring finger protein 141
Structure deposition date
2017-04-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
0
Peptide accession
Q8WVD5
Residue number A
177
Residue number B
188
Peptide name
RING finger protein 141
Ligandability
Cysteine 177 of RING finger protein 141
Cysteine 188 of RING finger protein 141
2ecn A 19 A 21
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 156 and 158 (19 and 21 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2ecn
Structure name
solution structure of the ring domain of the human ring finger protein 141
Structure deposition date
2007-02-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
1
Peptide accession
Q8WVD5
Residue number A
156
Residue number B
158
Peptide name
RING finger protein 141
Ligandability
Cysteine 156 of RING finger protein 141
Cysteine 158 of RING finger protein 141
2ecn A 19 A 40
A redox-regulated disulphide may form within RING finger protein 141 between cysteines 156 and 177 (19 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 ?
43
PDB code
2ecn
Structure name
solution structure of the ring domain of the human ring finger protein 141
Structure deposition date
2007-02-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
1
Peptide accession
Q8WVD5
Residue number A
156
Residue number B
177
Peptide name
RING finger protein 141
Ligandability
Cysteine 156 of RING finger protein 141
Cysteine 177 of RING finger protein 141
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