Elongation factor 1-alpha 2
8b6z A 363 A 370
A redox-regulated disulphide may form within Elongation factor 1-alpha 2 between cysteines 363 and 370. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
8b6z
Structure name
cryoem structure of extended eef1a bound to the ribosome in the classical pre state
Structure deposition date
2022-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
88
Peptide accession
Q05639
Residue number A
363
Residue number B
370
Peptide name
Elongation factor 1-alpha 2
Ligandability
Cysteine 363 of Elongation factor 1-alpha 2
Cysteine 370 of Elongation factor 1-alpha 2
8b6z A 363 A 411
A redox-regulated disulphide may form within Elongation factor 1-alpha 2 between cysteines 363 and 411. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
8b6z
Structure name
cryoem structure of extended eef1a bound to the ribosome in the classical pre state
Structure deposition date
2022-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
Q05639
Residue number A
363
Residue number B
411
Peptide name
Elongation factor 1-alpha 2
Ligandability
Cysteine 363 of Elongation factor 1-alpha 2
Cysteine 411 of Elongation factor 1-alpha 2
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