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Monoclinic crystal structure of red abalone lysin at 2.11 a resolution

Analyse Monoclinic crystal structure of red abalone lysin at 2.11 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5II9
Type
protein
Length
784 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Egg-lysin
UniProt
P04552
Pockets
4 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, E, FEgg-lysinprotein13173% helix, 0% strandP04552
C, DEgg-lysinprotein13071% helix, 0% strandP04552

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15850.720.8059empty
27370.710.7747empty
32460.650.8231empty
41670.390.7222empty

Interfaces

4 interfaces between chains.

  • A–E · 801 Ų buried · 9 hydrogen bonds · protein-protein
  • A–C · 797 Ų buried · 9 hydrogen bonds · protein-protein
  • D–E · 205 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 48 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 5II9 · Monoclinic crystal structure of red abalone lysin at 2.11 A resolution · the same entry in another collection · chain F against F, TM-score 1.00
  • P04552 · AlphaFold monomer V2.0 prediction for egg-lysin (P04552) · a predicted model of the same protein · chain C against A, TM-score 0.95

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