Research workbench

Crystal structure of the leptospiral antigen LP49

Analyse Crystal structure of the leptospiral antigen LP49 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BWS
Type: protein
Length: 814 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein LP49
UniProt: Q8F0X1
Ligands: SO4
Pockets: 11 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein LP49	protein	407	3% helix, 55% strand	Q8F0X1

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	409	0.65	0.78	34	empty
2	376	0.62	0.78	36	empty
3	471	0.59	0.74	49	empty
4	167	0.54	0.79	26	SO4
5	183	0.53	0.78	26	SO4

Interfaces

1 interface between chains.

A–B · 644 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified, 2 disulfide (engineered, disulfide).

Compared structures

3BWS · Crystal structure of the leptospiral antigen Lp49 · 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 Q8F0X1
Elsewhere: RCSB PDB 3BWS · PDBe 3BWS · UniProt Q8F0X1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.