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Crystal structure of trk-a complexed with a selective inhibitor CH7057288

Analyse Crystal structure of trk-a complexed with a selective inhibitor CH7057288 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WR7
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: High affinity nerve growth factor receptor
EC: 2.7.10.1
UniProt: P04629
Ligands: RCH
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	High affinity nerve growth factor receptor (EC 2.7.10.1)	protein	302	36% helix, 17% strand	P04629

Ligands and binding sites

RCH · N-tert-butyl-2-[2-[6,6-dimethyl-8-(methylsulfonylamino)-11-oxidanylidene-naphtho[2,3-b][1]benzofuran-3-yl]ethynyl]-6-methyl-pyridine-4-carboxamide · ligand · 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	593	0.73	0.80	65	RCH

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

5WR7 · Crystal structure of Trk-A complexed with a selective inhibitor CH7057288 · 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 P04629
Elsewhere: RCSB PDB 5WR7 · PDBe 5WR7 · UniProt P04629

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