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Crystal structure of C-met kinase domain in complex with 4-((6-(4- fluorophenyl)-(1,2,4)TRIAZOLO(4,3-B)(1,2,4)TRIAZIN-3-YL)METHYL)PHENOL

Analyse Crystal structure of C-met kinase domain in complex with 4-((6-(4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AP7
Type: protein
Length: 289 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hepatocyte growth factor receptor
EC: 2.7.10.1
UniProt: P08581
Ligands: F47
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hepatocyte growth factor receptor (EC 2.7.10.1)	protein	289	42% helix, 15% strand	P08581

Ligands and binding sites

F47 · 4-[[6-(4-fluorophenyl)-[1,2,4]triazolo[4,3-b][1,2,4]triazin-3-yl]methyl]phenol · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	169	0.64	0.85	27	F47
2	167	0.51	0.78	23	empty

Compared structures

4AP7 · Crystal structure of C-MET kinase domain in complex with 4-((6-(4… · 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 P08581
Elsewhere: RCSB PDB 4AP7 · PDBe 4AP7 · UniProt P08581

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