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HtrA2 Pathogenic Mutant

Analyse HtrA2 Pathogenic Mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WYN
Type: protein
Length: 293 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.05
Source: Homo sapiens
Molecule: Serine protease HTRA2, mitochondrial
EC: 3.4.21.108
UniProt: O43464
Ligands: CL
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · resolution 2.05 · 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	293	19% helix, 40% strand	O43464

Ligands and binding sites

CL · Chloride ion · ion · 6 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

4 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	183	0.64	0.84	28	CL
2	53	0.47	0.85	23	CL
3	87	0.39	0.77	20	CL
4	62	0.31	0.75	16	CL

Compared structures

5WYN · HTRA2 pathogenic 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 0.99

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 5WYN · PDBe 5WYN · UniProt O43464

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