Eukaryotic translation initiation factor 5
Intramolecular
Cysteine 102 and cysteine 122
Cysteine 99 and cysteine 122
Cysteine 99 and cysteine 102
Cysteine 99 and cysteine 125
Cysteine 102 and cysteine 125
Cysteine 122 and cysteine 125
Cysteine 99 and cysteine 138
Cysteine 59 and cysteine 138
2e9h A 109 A 129
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 5 between cysteines 102 and 122 (109 and 129 respectively in this structure).
Details
Redox score ?
90
PDB code
2e9h
Structure name
solution structure of the eif-5_eif-2b domain from human eukaryotic translation initiation factor 5
Structure deposition date
2007-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
5
% buried
0
Peptide accession
P55010
Residue number A
102
Residue number B
122
Peptide name
Eukaryotic translation initiation factor 5
Ligandability
Cysteine 102 of Eukaryotic translation initiation factor 5
Cysteine 122 of Eukaryotic translation initiation factor 5
2e9h A 106 A 129
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 5 between cysteines 99 and 122 (106 and 129 respectively in this structure).
Details
Redox score ?
89
PDB code
2e9h
Structure name
solution structure of the eif-5_eif-2b domain from human eukaryotic translation initiation factor 5
Structure deposition date
2007-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
4
Peptide accession
P55010
Residue number A
99
Residue number B
122
Peptide name
Eukaryotic translation initiation factor 5
Ligandability
Cysteine 99 of Eukaryotic translation initiation factor 5
Cysteine 122 of Eukaryotic translation initiation factor 5
2e9h A 106 A 109
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 5 between cysteines 99 and 102 (106 and 109 respectively in this structure).
Details
Redox score ?
82
PDB code
2e9h
Structure name
solution structure of the eif-5_eif-2b domain from human eukaryotic translation initiation factor 5
Structure deposition date
2007-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
4
Peptide accession
P55010
Residue number A
99
Residue number B
102
Peptide name
Eukaryotic translation initiation factor 5
Ligandability
Cysteine 99 of Eukaryotic translation initiation factor 5
Cysteine 102 of Eukaryotic translation initiation factor 5
2e9h A 106 A 132
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 5 between cysteines 99 and 125 (106 and 132 respectively in this structure).
Details
Redox score ?
81
PDB code
2e9h
Structure name
solution structure of the eif-5_eif-2b domain from human eukaryotic translation initiation factor 5
Structure deposition date
2007-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
4
Peptide accession
P55010
Residue number A
99
Residue number B
125
Peptide name
Eukaryotic translation initiation factor 5
Ligandability
Cysteine 99 of Eukaryotic translation initiation factor 5
Cysteine 125 of Eukaryotic translation initiation factor 5
2e9h A 109 A 132
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 5 between cysteines 102 and 125 (109 and 132 respectively in this structure).
Details
Redox score ?
76
PDB code
2e9h
Structure name
solution structure of the eif-5_eif-2b domain from human eukaryotic translation initiation factor 5
Structure deposition date
2007-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
10
% buried
0
Peptide accession
P55010
Residue number A
102
Residue number B
125
Peptide name
Eukaryotic translation initiation factor 5
Ligandability
Cysteine 102 of Eukaryotic translation initiation factor 5
Cysteine 125 of Eukaryotic translation initiation factor 5
2g2k A 122 A 125
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 5 between cysteines 122 and 125. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
2g2k
Structure name
nmr structure of an n-terminal fragment of the eukaryotic initiation factor 5 (eif5)
Structure deposition date
2006-02-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
P55010
Residue number A
122
Residue number B
125
Peptide name
Eukaryotic translation initiation factor 5
Ligandability
Cysteine 122 of Eukaryotic translation initiation factor 5
Cysteine 125 of Eukaryotic translation initiation factor 5
2g2k A 99 A 138
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 5 between cysteines 99 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
2g2k
Structure name
nmr structure of an n-terminal fragment of the eukaryotic initiation factor 5 (eif5)
Structure deposition date
2006-02-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
18
Peptide accession
P55010
Residue number A
99
Residue number B
138
Peptide name
Eukaryotic translation initiation factor 5
Ligandability
Cysteine 99 of Eukaryotic translation initiation factor 5
Cysteine 138 of Eukaryotic translation initiation factor 5
2e9h A 66 A 145
A redox-regulated disulphide may form within Eukaryotic translation initiation factor 5 between cysteines 59 and 138 (66 and 145 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
2e9h
Structure name
solution structure of the eif-5_eif-2b domain from human eukaryotic translation initiation factor 5
Structure deposition date
2007-01-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
17
Peptide accession
P55010
Residue number A
59
Residue number B
138
Peptide name
Eukaryotic translation initiation factor 5
Ligandability
Cysteine 59 of Eukaryotic translation initiation factor 5
Cysteine 138 of Eukaryotic translation initiation factor 5
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