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Single particle electron microscopy of pilq dodecameric complexes from neisseria meningitidis.

Analyse Single particle electron microscopy of pilq dodecameric complexes from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4AV2
Type
protein
Length
4,272 residues
Chains
24
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Type IV pilus biogenesis and competence protein pilq; Pilp protein
UniProt
Q70M91, Q7DD77
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 2 distinct chains · 21% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LType IV pilus biogenesis and competence protein pilqprotein27426% helix, 33% strandQ70M91
M, N, O, P, Q, R, S, T, U, V, W, XPilp proteinprotein825% helix, 56% strandQ7DD77

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110860.820.83114empty
28690.800.8389empty
310530.800.82108empty
45800.760.8265empty
55720.750.8256empty

Interfaces

24 interfaces between chains.

  • J–K · 1824 Ų buried · 25 hydrogen bonds · protein-protein
  • K–L · 1824 Ų buried · 26 hydrogen bonds · protein-protein
  • C–D · 1823 Ų buried · 25 hydrogen bonds · protein-protein
  • B–C · 1823 Ų buried · 25 hydrogen bonds · protein-protein
  • A–B · 1823 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 4AV2 · Single particle electron microscopy of PilQ dodecameric complexes from Neisseria… · the same entry in another collection · chain A against A, TM-score 1.00

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