Research workbench

HTRA2 exposed (L266R, F303A) mutant

Analyse HTRA2 exposed (L266R, F303A) mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TO1
Type: protein
Length: 295 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine protease HTRA2, mitochondrial
EC: 3.4.21.108
UniProt: O43464
Ligands: CL
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine protease HTRA2, mitochondrial (EC 3.4.21.108)	protein	295	19% helix, 40% strand	O43464

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.27	0.74	14	empty

Compared structures

5TO1 · HtrA2 exposed (L266R, F303A) mutant · the same entry in another collection · chain A against A, TM-score 1.00
O43464 · AlphaFold monomer V2.0 prediction for serine protease HTRA2, mitochondrial (O43464) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 O43464
Elsewhere: RCSB PDB 5TO1 · PDBe 5TO1 · UniProt O43464

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