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Cross-alpha amyloid-like structure alphaaml

Analyse Cross-alpha amyloid-like structure alphaaml in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6C51
Type
protein
Length
99 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cross-alpha amyloid-like structure alphaaml
Ligands
ACE, PO4, NH2

Structure

x-ray diffraction · 2 distinct chains · 90% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, BCross-alpha amyloid-like structure alphaamlprotein2588% helix, 0% strand—
DCross-alpha amyloid-like structure alphaamlprotein2492% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · 4 copies · chains A, C, B, D
  • PO4 · Phosphate ion · ion · 6 copies · chains A, C, B, D
  • NH2 · Amino group · ion · 3 copies · chains A, C, B, D
  • MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains D

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

Interfaces

6 interfaces between chains.

  • A–B · 529 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 513 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 381 Ų buried · 2 hydrogen bonds · protein-protein
  • B–D · 179 Ų buried · 0 hydrogen bonds · protein-protein
  • C–B · 71 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 covalent (covalent ligand).

Compared structures

  • 6C51 · Cross-alpha Amyloid-like Structure alphaAmL · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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