MolNFT v1 · #85994 · protein

Crystal structure of trkb kinase domain in complex with EX429

4AT4 · BDNF/NT-3 growth factors receptor: “Crystal structure of trkb kinase domain in complex with EX429”. X-ray diffraction, 1 ligand (T6E), 2 pockets (best druggability 0.72). MolNFT v1 #85994 on GenesisL1: 3D structure, binding sites…

PDB: 4AT4
Type: protein
Length: 292 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BDNF/NT-3 growth factors receptor
EC: 2.7.10.1
UniProt: Q16620
Ligands: T6E
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BDNF/NT-3 growth factors receptor (EC 2.7.10.1)	protein	292	45% helix, 18% strand	Q16620

Ligands and binding sites

T6E · 1-[4-(4-aminothieno[2,3-d]pyrimidin-5-yl)phenyl]-3-[2-fluoro-5-(trifluoromethyl)phenyl]urea · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	414	0.72	0.82	46	T6E
2	64	0.32	0.75	18	empty

Compared structures

4AT4 · Crystal structure of trkb kinase domain in complex with EX429 · the same entry in another collection · chain A against A, TM-score 1.00
Q16620 · AlphaFold monomer V2.0 prediction for BDNF/NT-3 growth factors receptor (Q16620) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q16620
Elsewhere: RCSB PDB 4AT4 · PDBe 4AT4 · UniProt Q16620

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