Research workbench

Crystal structure of a chimeric C-src-SH3 domain

Analyse Crystal structure of a chimeric C-src-SH3 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LE9
Type: protein
Length: 59 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene tyrosine-protein kinase src
EC: 2.7.10.2
UniProt: P00523
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proto-oncogene tyrosine-protein kinase src (EC 2.7.10.2)	protein	59	10% helix, 31% strand	P00523

Ligands and binding sites

PGE · Triethylene glycol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	255	0.51	0.75	32	empty

Compared structures

4LE9 · Crystal structure of a chimeric c-Src-SH3 domain · 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 P00523
Elsewhere: RCSB PDB 4LE9 · PDBe 4LE9 · UniProt P00523

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.