a tool for identifying drug-targetable redox-active disulphides

Kinesin family member 13A

Intramolecular

Cysteine 513 and cysteine 520

A redox-regulated disulphide may form within Kinesin family member 13A between cysteines 513 and 520 (128 and 135 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

Structure name

crystal structure of the cc1-fha tandem of kinesin-3 kif13a

Structure deposition date

2015-09-02

Thiol separation (Å)

9

Half-sphere exposure sum ?

51

Minimum pK_a ?

9

% buried

8

Peptide accession

Residue number A

513

Residue number B

520

Peptide name

Kinesin family member 13A

Ligandability

Cysteine 513 of Kinesin family member 13A

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 520 of Kinesin family member 13A

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.

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