› 6ds5

Electron Microscopy
3.8Å resolution

Cryo EM structure of human SEIPIN

Released:
DOI: 10.2210/pdb6ds5/pdb
PDB entry 6ds5 coloured by chain, front view.
PDB entry 6ds5 coloured by chain, side view.
PDB entry 6ds5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human SEIPIN Binds Anionic Phospholipids.
Yan R, Qian H, Lukmantara I, Gao M, Du X, Yan N, Yang H
Dev Cell 47 248-256.e4 (2018)
PMID: 30293840
Related structures: EMD-8909

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
homo undecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188514 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Seipin Chains: A, B, C, D, E, F, G, H, I, J, K
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K
Length: 409 amino acids
Theoretical weight: 45.77 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q96G97 (Residues: 2-398; Coverage: 100%)
Gene name: BSCL2
Sequence domains: Putative adipose-regulatory protein (Seipin)

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.8Å
Relevant EMDB volumes: EMD-8909
Expression system: Homo sapiens

Quick links

Citations

28 review citations

Dynamics and functions of lipid droplets.
Olzmann et al. (2019)
27 more

10 mentions without citation

Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels.
Egea PF. (2021)
9 more