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Crystal structure of P. falciparum LIPL1 in complex lipoate

Analyse Crystal structure of P. falciparum LIPL1 in complex lipoate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T8U
Type: protein
Length: 669 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipoate-protein ligase 1
EC: 2.7.7.63
UniProt: Q8IEG9
Ligands: LPA
Pockets: 15 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipoate-protein ligase 1 (EC 2.7.7.63)	protein	333	34% helix, 24% strand	Q8IEG9
B	Lipoate-protein ligase 1 (EC 2.7.7.63)	protein	336	35% helix, 25% strand	Q8IEG9

Ligands and binding sites

LPA · Lipoic acid · ligand · 2 copies · chains A, B

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

Pockets

15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	955	0.83	0.85	111	LPA
2	160	0.71	0.90	21	empty
3	55	0.55	0.88	14	empty
4	176	0.54	0.80	28	empty
5	52	0.52	0.87	13	empty

Interfaces

1 interface between chains.

A–B · 1363 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

5T8U · Crystal structure of P. falciparum LipL1 in complex lipoate · 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 Q8IEG9
Elsewhere: RCSB PDB 5T8U · PDBe 5T8U · UniProt Q8IEG9

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