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Crystal structure of plasmodium falciparum ADP-ribosylation factor 1

Analyse Crystal structure of plasmodium falciparum ADP-ribosylation factor 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LRP
Type: protein
Length: 181 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosylation factor 1
UniProt: Q94650
Ligands: GDP, MG, SO4
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ADP-ribosylation factor 1	protein	181	35% helix, 24% strand	Q94650

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
SO4 · Sulfate ion · ion · chains A

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

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	52	0.34	0.78	13	empty

Compared structures

3LRP · Crystal Structure of Plasmodium falciparum ADP-Ribosylation Factor 1 · the same entry in another collection · chain A against A, TM-score 1.00
Q94650 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor 1 (Q94650) · a predicted model of the same protein · chain A against A, TM-score 0.81

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 Q94650
Elsewhere: RCSB PDB 3LRP · PDBe 3LRP · UniProt Q94650

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