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Solution structure of the human fes SH2 domain

Analyse Solution structure of the human fes SH2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WQU
Type: protein
Length: 114 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene tyrosine-protein kinase FES/FPS
EC: 2.7.1.112
UniProt: P07332
Pockets: 1 · best druggability 0.31

Structure

solution nmr · 1 distinct chain · 19% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proto-oncogene tyrosine-protein kinase FES/FPS (EC 2.7.1.112)	protein	114	19% helix, 25% strand	P07332

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.31	0.75	13	empty

Compared structures

1WQU · Solution structure of the human FES SH2 domain · the same entry in another collection · chain A against A, TM-score 1.00
P07332 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase FES/FPS (P07332) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P07332
Elsewhere: RCSB PDB 1WQU · PDBe 1WQU · UniProt P07332

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