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Solution structure of lipase binding domain LID1 of foldase from pseudomonas aeruginosa

Analyse Solution structure of lipase binding domain LID1 of foldase from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OVM
Type: protein
Length: 82 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase chaperone
UniProt: Q01725
Pockets: 1 · best druggability 0.56

Structure

solution nmr · 1 distinct chain · 46% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipase chaperone	protein	82	46% helix, 0% strand	Q01725

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	116	0.56	0.83	24	empty

Compared structures

5OVM · Solution structure of lipase binding domain LID1 of foldase from Pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
Q01725 · AlphaFold monomer V2.0 prediction for lipase chaperone (Q01725) · a predicted model of the same protein · chain A against A, TM-score 0.65

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 Q01725
Elsewhere: RCSB PDB 5OVM · PDBe 5OVM · UniProt Q01725

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