Research workbench

C-term tail segment of human tyrosine kinase (258-533)

Analyse C-term tail segment of human tyrosine kinase (258-533) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YI6
Type: protein
Length: 552 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene tyrosine-protein kinase src
EC: 2.7.1.112
UniProt: P12931
Pockets: 6 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Proto-oncogene tyrosine-protein kinase src (EC 2.7.1.112)	protein	276	39% helix, 17% strand	P12931

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	531	0.70	0.80	65	empty
2	328	0.63	0.79	40	empty
3	442	0.63	0.77	52	empty
4	95	0.43	0.79	21	empty
5	50	0.35	0.79	15	empty

Interfaces

1 interface between chains.

A–B · 731 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

1YI6 · C-term tail segment of human tyrosine kinase (258-533) · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P12931
Elsewhere: RCSB PDB 1YI6 · PDBe 1YI6 · UniProt P12931

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