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Plasmepsin II complexed with a highly active achiral inhibitor

Analyse Plasmepsin II complexed with a highly active achiral inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BJU
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Plasmepsin II
EC: 3.4.23.39
UniProt: P46925
Ligands: IH4
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Plasmepsin II (EC 3.4.23.39)	protein	329	13% helix, 48% strand	P46925

Ligands and binding sites

IH4 · N-(R-carboxy-ethyl)-alpha-(S)-(2-phenylethyl) · ligand · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	448	0.67	0.78	51	IH4
2	133	0.49	0.79	18	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2BJU · Plasmepsin II complexed with a highly active achiral inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
P46925 · AlphaFold monomer V2.0 prediction for plasmepsin-2 (P46925) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P46925
Elsewhere: RCSB PDB 2BJU · PDBe 2BJU · UniProt P46925

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