Artemin
Intermolecular
Cysteine 187 and cysteine 187
Intramolecular
Cysteine 154 and cysteine 218
Cysteine 123 and cysteine 188
Cysteine 150 and cysteine 216
Cysteine 123 and cysteine 218
Cysteine 123 and cysteine 154
Cysteine 123 and cysteine 216
Cysteine 188 and cysteine 216
Cysteine 188 and cysteine 218
Cysteine 154 and cysteine 188
More...Cysteine 150 and cysteine 188
Cysteine 123 and cysteine 150
Cysteine 154 and cysteine 187
Cysteine 150 and cysteine 218
Cysteine 187 and cysteine 218
Cysteine 216 and cysteine 218
Cysteine 154 and cysteine 216
Cysteine 187 and cysteine 188
Cysteine 123 and cysteine 187
Cysteine 150 and cysteine 154
2gyr A 69 B 69
A redox-regulated disulphide may form between two units of Artemin at cysteines 187 and 187 (69 and 69 respectively in this structure).
Details
Redox score ?
79
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
Artemin
Peptide B name
Artemin
Peptide A accession
Q5T4W7
Peptide B accession
Q5T4W7
Peptide A residue number
187
Peptide B residue number
187
Ligandability
2gyz A 36 A 100
A redox-regulated disulphide may form within Artemin between cysteines 154 and 218 (36 and 100 respectively in this structure).
Details
Redox score ?
92
PDB code
2gyz
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
154
Residue number B
218
Peptide name
Artemin
Ligandability
Cysteine 154 of Artemin
Cysteine 218 of Artemin
2gyr E 5 E 70
A redox-regulated disulphide may form within Artemin between cysteines 123 and 188 (5 and 70 respectively in this structure).
Details
Redox score ?
87
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
123
Residue number B
188
Peptide name
Artemin
Ligandability
Cysteine 123 of Artemin
Cysteine 188 of Artemin
2gyr D 32 D 98
A redox-regulated disulphide may form within Artemin between cysteines 150 and 216 (32 and 98 respectively in this structure).
Details
Redox score ?
85
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
150
Residue number B
216
Peptide name
Artemin
Ligandability
Cysteine 150 of Artemin
Cysteine 216 of Artemin
2gyr E 5 E 100
A redox-regulated disulphide may form within Artemin between cysteines 123 and 218 (5 and 100 respectively in this structure).
Details
Redox score ?
83
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
123
Residue number B
218
Peptide name
Artemin
Ligandability
Cysteine 123 of Artemin
Cysteine 218 of Artemin
2gyr E 5 E 36
A redox-regulated disulphide may form within Artemin between cysteines 123 and 154 (5 and 36 respectively in this structure).
Details
Redox score ?
76
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
123
Residue number B
154
Peptide name
Artemin
Ligandability
Cysteine 123 of Artemin
Cysteine 154 of Artemin
2gyz A 5 A 98
A redox-regulated disulphide may form within Artemin between cysteines 123 and 216 (5 and 98 respectively in this structure).
Details
Redox score ?
72
PDB code
2gyz
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
123
Residue number B
216
Peptide name
Artemin
Ligandability
Cysteine 123 of Artemin
Cysteine 216 of Artemin
2gyr B 70 B 98
A redox-regulated disulphide may form within Artemin between cysteines 188 and 216 (70 and 98 respectively in this structure).
Details
Redox score ?
71
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
188
Residue number B
216
Peptide name
Artemin
Ligandability
Cysteine 188 of Artemin
Cysteine 216 of Artemin
2gyr A 70 A 100
A redox-regulated disulphide may form within Artemin between cysteines 188 and 218 (70 and 100 respectively in this structure).
Details
Redox score ?
69
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
188
Residue number B
218
Peptide name
Artemin
Ligandability
Cysteine 188 of Artemin
Cysteine 218 of Artemin
2gyr B 36 B 70
A redox-regulated disulphide may form within Artemin between cysteines 154 and 188 (36 and 70 respectively in this structure).
Details
Redox score ?
69
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
154
Residue number B
188
Peptide name
Artemin
Ligandability
Cysteine 154 of Artemin
Cysteine 188 of Artemin
2gyr E 32 E 70
A redox-regulated disulphide may form within Artemin between cysteines 150 and 188 (32 and 70 respectively in this structure).
Details
Redox score ?
65
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
150
Residue number B
188
Peptide name
Artemin
Ligandability
Cysteine 150 of Artemin
Cysteine 188 of Artemin
2gyr C 5 C 32
A redox-regulated disulphide may form within Artemin between cysteines 123 and 150 (5 and 32 respectively in this structure).
Details
Redox score ?
61
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
123
Residue number B
150
Peptide name
Artemin
Ligandability
Cysteine 123 of Artemin
Cysteine 150 of Artemin
2gyr E 36 E 69
A redox-regulated disulphide may form within Artemin between cysteines 154 and 187 (36 and 69 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
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
154
Residue number B
187
Peptide name
Artemin
Ligandability
Cysteine 154 of Artemin
Cysteine 187 of Artemin
2gyz A 32 A 100
A redox-regulated disulphide may form within Artemin between cysteines 150 and 218 (32 and 100 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
2gyz
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
150
Residue number B
218
Peptide name
Artemin
Ligandability
Cysteine 150 of Artemin
Cysteine 218 of Artemin
2gyr F 69 F 100
A redox-regulated disulphide may form within Artemin between cysteines 187 and 218 (69 and 100 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
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
187
Residue number B
218
Peptide name
Artemin
Ligandability
Cysteine 187 of Artemin
Cysteine 218 of Artemin
2gh0 C 216 C 218
A redox-regulated disulphide may form within Artemin between cysteines 216 and 218. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2gh0
Structure name
growth factor/receptor complex
Structure deposition date
2006-03-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
216
Residue number B
218
Peptide name
Artemin
Ligandability
Cysteine 216 of Artemin
Cysteine 218 of Artemin
2gyr B 36 B 98
A redox-regulated disulphide may form within Artemin between cysteines 154 and 216 (36 and 98 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
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
154
Residue number B
216
Peptide name
Artemin
Ligandability
Cysteine 154 of Artemin
Cysteine 216 of Artemin
2gyr D 69 D 70
A redox-regulated disulphide may form within Artemin between cysteines 187 and 188 (69 and 70 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
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
187
Residue number B
188
Peptide name
Artemin
Ligandability
Cysteine 187 of Artemin
Cysteine 188 of Artemin
2gyr A 5 A 69
A redox-regulated disulphide may form within Artemin between cysteines 123 and 187 (5 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
123
Residue number B
187
Peptide name
Artemin
Ligandability
Cysteine 123 of Artemin
Cysteine 187 of Artemin
2gyr E 32 E 36
A redox-regulated disulphide may form within Artemin between cysteines 150 and 154 (32 and 36 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
2gyr
Structure name
crystal structure of human artemin
Structure deposition date
2006-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5T4W7
Residue number A
150
Residue number B
154
Peptide name
Artemin
Ligandability
Cysteine 150 of Artemin
Cysteine 154 of Artemin
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