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Cryo-EM structure of lipid droplet formation protein SEIPIN/BSCL2

Analyse Cryo-EM structure of lipid droplet formation protein SEIPIN/BSCL2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MLU
Type: protein
Length: 306 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Seipin
UniProt: Q9V3X4
Pockets: 7 · best druggability 0.70

Structure

electron microscopy · 1 distinct chain · 19% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Seipin	protein	153	19% helix, 34% strand	Q9V3X4

Pockets

7 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	69	0.70	0.95	30	empty
2	73	0.68	0.93	28	empty
3	163	0.52	0.78	23	empty
4	202	0.51	0.76	23	empty
5	115	0.46	0.79	22	empty

Interfaces

1 interface between chains.

A–B · 1025 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6MLU · Cryo-EM structure of lipid droplet formation protein Seipin/BSCL2 · the same entry in another collection · chain A against A, TM-score 1.00
Q9V3X4 · AlphaFold monomer V2.0 prediction for seipin (Q9V3X4) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 Q9V3X4
Elsewhere: RCSB PDB 6MLU · PDBe 6MLU · UniProt Q9V3X4

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