MolNFT v1 · #135075 · protein

HTRA2 S142D mutant

5TNZ · Serine protease HTRA2, mitochondrial: “HTRA2 S142D mutant”. X-ray diffraction, 1 ligand (NA), 2 pockets (best druggability 0.46). MolNFT v1 #135075 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5TNZ
Type: protein
Length: 293 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: NA
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine protease HTRA2, mitochondrial (EC 3.4.21.108)	protein	293	19% helix, 41% strand	O43464

Ligands and binding sites

NA · Sodium ion · metal · 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

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.46	0.80	21	empty
2	53	0.28	0.74	12	empty

Compared structures

5TNZ · HtrA2 S142D 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 5TNZ · PDBe 5TNZ · UniProt O43464

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