Selenocysteine-specific elongation factor
Intramolecular
Cysteine 422 and cysteine 426
Cysteine 93 and cysteine 130 L
Cysteine 231 and cysteine 289 L
Cysteine 93 and cysteine 138 L
Cysteine 130 and cysteine 138 L
Cysteine 130 and cysteine 442 L
Cysteine 304 and cysteine 422
5izl A 422 A 426
A redox-regulated disulphide may form within Selenocysteine-specific elongation factor between cysteines 422 and 426.
Details
Redox score ?
70
PDB code
5izl
Structure name
the crystal structure of human eefsec in complex with gdpcp
Structure deposition date
2016-03-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
81
Peptide accession
P57772
Residue number A
422
Residue number B
426
Peptide name
Selenocysteine-specific elongation factor
Ligandability
Cysteine 422 of Selenocysteine-specific elongation factor
Cysteine 426 of Selenocysteine-specific elongation factor
5izm B 93 B 130
A redox-regulated disulphide may form within Selenocysteine-specific elongation factor between cysteines 93 and 130. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5izm
Structure name
the crystal structure of human eefsec in complex with gdpnp
Structure deposition date
2016-03-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
11
% buried
100
Peptide accession
P57772
Residue number A
93
Residue number B
130
Peptide name
Selenocysteine-specific elongation factor
Ligandability
Cysteine 93 of Selenocysteine-specific elongation factor
Cysteine 130 of Selenocysteine-specific elongation factor
5izl A 231 A 289
A redox-regulated disulphide may form within Selenocysteine-specific elongation factor between cysteines 231 and 289. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
5izl
Structure name
the crystal structure of human eefsec in complex with gdpcp
Structure deposition date
2016-03-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
32
Peptide accession
P57772
Residue number A
231
Residue number B
289
Peptide name
Selenocysteine-specific elongation factor
Ligandability
Cysteine 231 of Selenocysteine-specific elongation factor
Cysteine 289 of Selenocysteine-specific elongation factor
5izm B 93 B 138
A redox-regulated disulphide may form within Selenocysteine-specific elongation factor between cysteines 93 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5izm
Structure name
the crystal structure of human eefsec in complex with gdpnp
Structure deposition date
2016-03-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
97
Peptide accession
P57772
Residue number A
93
Residue number B
138
Peptide name
Selenocysteine-specific elongation factor
Ligandability
Cysteine 93 of Selenocysteine-specific elongation factor
Cysteine 138 of Selenocysteine-specific elongation factor
5izm A 130 A 138
A redox-regulated disulphide may form within Selenocysteine-specific elongation factor between cysteines 130 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5izm
Structure name
the crystal structure of human eefsec in complex with gdpnp
Structure deposition date
2016-03-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
94
Peptide accession
P57772
Residue number A
130
Residue number B
138
Peptide name
Selenocysteine-specific elongation factor
Ligandability
Cysteine 130 of Selenocysteine-specific elongation factor
Cysteine 138 of Selenocysteine-specific elongation factor
5izl B 130 B 442
A redox-regulated disulphide may form within Selenocysteine-specific elongation factor between cysteines 130 and 442. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
5izl
Structure name
the crystal structure of human eefsec in complex with gdpcp
Structure deposition date
2016-03-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
86
Peptide accession
P57772
Residue number A
130
Residue number B
442
Peptide name
Selenocysteine-specific elongation factor
Ligandability
Cysteine 130 of Selenocysteine-specific elongation factor
Cysteine 442 of Selenocysteine-specific elongation factor
5izk A 304 A 422
A redox-regulated disulphide may form within Selenocysteine-specific elongation factor between cysteines 304 and 422. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
5izk
Structure name
the crystal structure of human eefsec in complex with gdp
Structure deposition date
2016-03-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
68
Peptide accession
P57772
Residue number A
304
Residue number B
422
Peptide name
Selenocysteine-specific elongation factor
Ligandability
Cysteine 304 of Selenocysteine-specific elongation factor
Cysteine 422 of Selenocysteine-specific elongation factor
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