Tyrosine-protein kinase Fgr

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Tyrosine-protein kinase Fgr at cysteines 415 and 415 (419 and 419 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7uy0

Structure name

crystal structure of human fgr tyrosine kinase in complex with a- 419259

Structure deposition date

2022-05-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Tyrosine-protein kinase Fgr

Peptide B name

Tyrosine-protein kinase Fgr

Peptide A accession

P09769

Peptide B accession

P09769

Peptide A residue number

415

Peptide B residue number

415

Ligandability

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.

A redox-regulated disulphide may form within Tyrosine-protein kinase Fgr between cysteines 479 and 483 (483 and 487 respectively in this structure).