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X-ray crystallographic structure of a covalent trimer derived from a- beta 17_36. X-ray diffractometer data set. (ORN)CVF(MEA)CED(ORN) AIIGL(ORN)V.

Analyse X-ray crystallographic structure of a covalent trimer derived from a- beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5SUS
Type
protein
Length
64 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
16MER a-beta peptide: orn-cys-val-phe-mea-cys-glu-asp-orn- ala-ile-ile-gly-leu-orn-val
Ligands
NA, CL

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 63% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D16MER a-beta peptide: orn-cys-val-phe-mea-cys-glu-asp-orn- ala-ile-ile-gly-leu-orn-valprotein160% helix, 63% strand—

Ligands and binding sites

  • NA · Sodium ion · metal · chains C
  • CL · Chloride ion · ion · chains B

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

Interfaces

4 interfaces between chains.

  • A–B · 241 Ų buried · 1 hydrogen bond · protein-protein
  • B–D · 192 Ų buried · 4 hydrogen bonds · protein-protein
  • C–D · 184 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 176 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (nonstandard).

Compared structures

  • 5SUS · X-ray crystallographic structure of a covalent trimer derived from A-beta 17_36. X-ray… · the same entry in another collection · chain A against A, TM-score 1.00

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