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Crystal structure of PFRH5, an essential P. falciparum ligand for invasion of human erythrocytes

Analyse Crystal structure of PFRH5, an essential P. falciparum ligand for invasion of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WAT
Type: protein
Length: 332 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PFRH5
Ligands: NAG
Pockets: 6 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PFRH5	protein	332	73% helix, 3% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
IMD · Imidazole · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 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	150	0.51	0.78	23	empty
2	78	0.48	0.83	21	IMD
3	93	0.40	0.77	21	empty
4	91	0.36	0.75	20	empty
5	89	0.36	0.75	13	empty

Modifications

Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

4WAT · Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 4WAT · PDBe 4WAT

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