Research workbench

Lips and lipt, two metagenome-derived lipolytic enzymes increase the diversity of known lipase and esterase families

Analyse Lips and lipt, two metagenome-derived lipolytic enzymes increase the diversity… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FBM
Type: protein
Length: 502 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lips lipolytic enzyme
Ligands: BR
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lips lipolytic enzyme	protein	252	37% helix, 16% strand	—
B	Lips lipolytic enzyme	protein	250	40% helix, 18% strand	—

Ligands and binding sites

BR · Bromide ion · ion · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.63	0.87	34	empty
2	60	0.35	0.77	13	empty
3	59	0.26	0.72	16	empty

Interfaces

1 interface between chains.

A–B · 1280 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4FBM · LipS and LipT, two metagenome-derived lipolytic enzymes increase the diversity of known… · 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
Elsewhere: RCSB PDB 4FBM · PDBe 4FBM

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