Research workbench

Serine Protease HtrA3, mutationally inactivated

Analyse Serine Protease HtrA3, mutationally inactivated in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RI0
Type: protein
Length: 704 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.272
Source: Homo sapiens
Molecule: Serine protease HTRA3
EC: 3.4.21.-
UniProt: P83110
Ligands: PO4
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · resolution 3.272 · 3 distinct chains · 15% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine protease HTRA3 (EC 3.4.21.-)	protein	306	15% helix, 41% strand	P83110
B	Serine protease HTRA3 (EC 3.4.21.-)	protein	202	14% helix, 44% strand	P83110
C	Serine protease HTRA3 (EC 3.4.21.-)	protein	196	16% helix, 40% strand	P83110

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · 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	210	0.68	0.86	36	empty
2	227	0.45	0.73	25	empty
3	56	0.30	0.75	15	empty
4	62	0.29	0.74	17	empty

Interfaces

3 interfaces between chains.

A–C · 930 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 912 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 898 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4RI0 · Serine protease HTRA3, mutationally inactivated · the same entry in another collection · chain A against A, TM-score 1.00
P83110 · AlphaFold monomer V2.0 prediction for serine protease HTRA3 (P83110) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P83110
Elsewhere: RCSB PDB 4RI0 · PDBe 4RI0 · UniProt P83110

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