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Crystal structure of braf kinase domain bound to belvarafenib

Analyse Crystal structure of braf kinase domain bound to belvarafenib in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XFP
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase B-RAF
UniProt: H7C560
Ligands: V1Y, CL
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase B-RAF	protein	272	39% helix, 18% strand	H7C560

Ligands and binding sites

V1Y · 4-amino-N-{1-[(3-chloro-2-fluorophenyl)amino]-6-methylisoquinolin-5-yl}thieno[3,2-d]pyrimidine-7-carboxamide · ligand · chains A
CL · Chloride ion · ion · 6 copies · 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	513	0.76	0.83	54	V1Y, CL
2	58	0.35	0.78	13	CL

Compared structures

6XFP · Crystal Structure of BRAF kinase domain bound to Belvarafenib · 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 H7C560
Elsewhere: RCSB PDB 6XFP · PDBe 6XFP · UniProt H7C560

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