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HTRA1 bound to an optimized peptide: NMR assignment of PDZ domain and ligand resonances

Analyse HTRA1 bound to an optimized peptide: NMR assignment of PDZ domain and ligand… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JOA
Type: protein
Length: 112 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine protease HTRA1; Peptide H1-C1
EC: 3.4.21.-
UniProt: Q92743
Pockets: 1 · best druggability 0.50

Structure

solution nmr · 2 distinct chains · 22% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine protease HTRA1 (EC 3.4.21.-)	protein	105	24% helix, 30% strand	Q92743
B	Peptide H1-C1	protein	7	0% helix, 43% strand	—

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	122	0.50	0.80	22	empty

Interfaces

1 interface between chains.

A–B · 559 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2JOA · HtrA1 bound to an optimized peptide: NMR assignment of PDZ domain and ligand resonances · the same entry in another collection · chain A against A, TM-score 1.00
Q92743 · AlphaFold monomer V2.0 prediction for serine protease HTRA1 (Q92743) · a predicted model of the same protein · chain A against A, TM-score 0.84

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 Q92743
Elsewhere: RCSB PDB 2JOA · PDBe 2JOA · UniProt Q92743

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