MolNFT v1 · #63908 · protein

Crystal structure of histo-aspartic protease (hap) from plasmodium falciparum

3FNS · Hap protein: “Crystal structure of histo-aspartic protease (hap) from plasmodium falciparum”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.84). MolNFT v1 #63908 on GenesisL1: 3D structure, binding sites and…

PDB: 3FNS
Type: protein
Length: 650 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hap protein
UniProt: Q8IM15
Ligands: ZN
Pockets: 4 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hap protein	protein	325	13% helix, 46% strand	Q8IM15

Ligands and binding sites

ZN · Zinc ion · metal · 6 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	837	0.84	0.86	107	empty
2	456	0.68	0.79	38	empty
3	418	0.66	0.79	34	empty
4	58	0.41	0.81	21	empty

Interfaces

1 interface between chains.

A–B · 2398 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3FNS · Crystal structure of histo-aspartic protease (HAP) from Plasmodium Falciparum · 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
Every structure of UniProt Q8IM15
Elsewhere: RCSB PDB 3FNS · PDBe 3FNS · UniProt Q8IM15

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