Research workbench

AMA1 from plasmodium falciparum

Analyse AMA1 from plasmodium falciparum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Z40
Type: protein
Length: 617 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apical membrane antigen 1 precursor
UniProt: Q7KQK5
Ligands: CL
Pockets: 5 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apical membrane antigen 1 precursor	protein	311	17% helix, 27% strand	Q7KQK5
E	Apical membrane antigen 1 precursor	protein	306	17% helix, 29% strand	Q7KQK5

Ligands and binding sites

CL · Chloride ion · ion · chains A

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

Pockets

5 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	914	0.78	0.80	82	empty
2	146	0.47	0.77	21	empty
3	98	0.44	0.79	14	empty
4	77	0.43	0.80	16	CL
5	66	0.38	0.78	22	empty

Interfaces

1 interface between chains.

A–E · 527 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

1Z40 · AMA1 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 Q7KQK5
Elsewhere: RCSB PDB 1Z40 · PDBe 1Z40 · UniProt Q7KQK5

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