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MolNFT v2 · #14187 · protein

structural model of human decay-accelerating factor bound to echovirus 7 from cryo-electron microscopy

1M11: “structural model of human decay-accelerating factor bound to echovirus 7 from cryo-electron microscopy”. Electron microscopy at 16.0, 2 pockets (best druggability 0.32). MolNFT v2 #14187 on GenesisL1: 3D structure, binding sites and…

PDB
1M11
Type
protein
Length
1,013 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
16.0
Source
Homo sapiens; Human echovirus 7
Molecule
decay-accelerating factor; Coat protein VP1; Coat protein VP2; Coat protein VP3
UniProt
P08174, Q914E0
Pockets
2 · best druggability 0.32

Structure

electron microscopy · resolution 16.0 · 4 distinct chains · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Rdecay-accelerating factorprotein2430% helix, 0% strandP08174
1Coat protein VP1protein2780% helix, 0% strandQ914E0
2Coat protein VP2protein2540% helix, 0% strandQ914E0
3Coat protein VP3protein2380% helix, 0% strandQ914E0

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1750.320.7229empty
2600.290.7218empty

Interfaces

3 interfaces between chains.

  • 1–3 · 612 Ų buried · 0 hydrogen bonds · protein-protein
  • 1–2 · 384 Ų buried · 0 hydrogen bonds · protein-protein
  • 2–3 · 236 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1M11 · Structural model of human decay-accelerating factor bound to echovirus 7 from… · the same entry in another collection · chain 1 against 1, TM-score 1.00
  • P08174 · AlphaFold monomer V2.0 prediction for complement decay-accelerating factor (P08174) · a predicted model of the same protein · chain R against A, TM-score 0.40

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