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Tetrameric coiled-coil structure of liprin-alpha2_H2

Analyse Tetrameric coiled-coil structure of liprin-alpha2_H2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7D2H
Type
protein
Length
228 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.2
Source
Homo sapiens
Molecule
Liprin-alpha-2
UniProt
O75334

Structure

x-ray diffraction · resolution 2.2 · 4 distinct chains · 93% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALiprin-alpha-2protein5793% helix, 0% strandO75334
BLiprin-alpha-2protein5591% helix, 0% strandO75334
CLiprin-alpha-2protein5695% helix, 0% strandO75334
DLiprin-alpha-2protein6095% helix, 0% strandO75334

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

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

Interfaces

6 interfaces between chains.

  • A–B · 1093 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 1066 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 725 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 692 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 532 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 7D2H · Tetrameric coiled-coil structure of liprin-ALPHA2_H2 · the same entry in another collection · chain D against D, TM-score 1.00
  • O75334 · AlphaFold monomer V2.0 prediction for liprin-alpha-2 (O75334) · a predicted model of the same protein · chain C against A, TM-score 0.94

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