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Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) in E. coli polar lipids

Analyse Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) in E.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3M9I
Type
protein
Length
220 residues
Chains
1
Method
electron crystallography
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.5
Source
Ovis aries
Molecule
Lens fiber major intrinsic protein
UniProt
Q6J8I9
Ligands
3PE
Pockets
2 · best druggability 0.42

Structure

electron crystallography · resolution 2.5 · 1 distinct chain · 67% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALens fiber major intrinsic proteinprotein22067% helix, 0% strandQ6J8I9

Ligands and binding sites

  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · ligand · 7 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11110.420.7722empty
21040.360.7425empty

Compared structures

  • 3M9I · Electron crystallographic structure of lens aquaporin-0 (AQP0) (lens mip) in E. COLI… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6J8I9 · AlphaFold monomer V2.0 prediction for lens fiber major intrinsic protein (Q6J8I9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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