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Amyloid fibril morphology II (in vitro) from murine SAA1.1 protein

Analyse Amyloid fibril morphology II (in vitro) from murine SAA1.1 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZCG
Type
protein
Length
888 residues
Chains
24
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serum amyloid a-2 protein
UniProt
P05367
Pockets
9 · best druggability 0.77

Structure

electron microscopy · 1 distinct chain · 0% helix, 84% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
L, O, I, N, H, K, E, J, D, G, A, F, C, B, P, S, M, R, T, W, Q, V, X, USerum amyloid a-2 proteinprotein370% helix, 84% strandP05367

Pockets

9 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12670.770.8930empty
22520.760.8930empty
31710.730.9136empty
41770.690.8836empty
55870.630.7540empty

Interfaces

90 interfaces between chains.

  • L–P · 1596 Ų buried · 53 hydrogen bonds · protein-protein
  • P–T · 1593 Ų buried · 53 hydrogen bonds · protein-protein
  • L–H · 1593 Ų buried · 53 hydrogen bonds · protein-protein
  • N–J · 1591 Ų buried · 50 hydrogen bonds · protein-protein
  • T–X · 1591 Ų buried · 53 hydrogen bonds · protein-protein

Compared structures

  • 6ZCG · Amyloid fibril morphology ii (in vitro) from murine SAA1.1 protein · the same entry in another collection · chain L against L, TM-score 1.00

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