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Crystal structure of plasmodium falciparum erythrocyte binding antigen 140 (pfeba-140/BAEBL)

Analyse Crystal structure of plasmodium falciparum erythrocyte binding antigen 140… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GF2
Type: protein
Length: 595 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Erythrocyte binding antigen 140
UniProt: Q8WS31
Pockets: 11 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Erythrocyte binding antigen 140	protein	595	67% helix, 2% strand	Q8WS31

Ligands and binding sites

GOL · Glycerol · additive · 15 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	552	0.69	0.78	58	empty
2	50	0.67	0.96	17	GOL
3	334	0.65	0.80	41	GOL
4	135	0.55	0.82	19	empty
5	108	0.40	0.76	18	GOL

Modifications

Observed in the structure: 13 disulfide (disulfide).

Compared structures

4GF2 · Crystal structure of Plasmodium falciparum Erythrocyte Binding Antigen 140… · 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 Q8WS31
Elsewhere: RCSB PDB 4GF2 · PDBe 4GF2 · UniProt Q8WS31

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