eEF1A lysine and N-terminal methyltransferase

Intramolecular

A redox-regulated disulphide may form within eEF1A lysine and N-terminal methyltransferase between cysteines 587 and 617. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5wcj

Structure name

crystal structure of human methyltransferase-like protein 13 in complex with sah

Structure deposition date

2017-06-30

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Q8N6R0

Residue number A

587

Residue number B

617

Peptide name

eEF1A lysine and N-terminal methyltransferase

Ligandability

Cysteine 587 of eEF1A lysine and N-terminal methyltransferase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 617 of eEF1A lysine and N-terminal methyltransferase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

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