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Al amyloid fibril from a lambda 3 light chain in conformation a

Analyse Al amyloid fibril from a lambda 3 light chain in conformation a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Z1O
Type
protein
Length
534 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lambda 3 immunoglobulin light chain fragment, residues 2- 116
Pockets
3 · best druggability 0.67

Structure

electron microscopy · 1 distinct chain · 0% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
D, E, F, C, B, ALambda 3 immunoglobulin light chain fragment, residues 2- 116protein890% helix, 46% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12180.670.8536empty
2580.630.9329empty
3750.300.7213empty

Interfaces

9 interfaces between chains.

  • C–B · 3691 Ų buried · 118 hydrogen bonds · protein-protein
  • D–C · 3688 Ų buried · 118 hydrogen bonds · protein-protein
  • B–A · 3687 Ų buried · 118 hydrogen bonds · protein-protein
  • D–E · 3684 Ų buried · 118 hydrogen bonds · protein-protein
  • E–F · 3684 Ų buried · 118 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 6Z1O · AL amyloid fibril from a lambda 3 light chain in conformation A · the same entry in another collection · chain D against D, TM-score 1.00

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