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Structural basis of bama-mediate outer membrane protein biogenesis

Analyse Structural basis of bama-mediate outer membrane protein biogenesis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4N75
Type
protein
Length
749 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Outer membrane protein assembly factor bama
UniProt
P0A940
Pockets
9 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOuter membrane protein assembly factor bamaprotein3794% helix, 53% strandP0A940
BOuter membrane protein assembly factor bamaprotein3704% helix, 56% strandP0A940

Pockets

9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111120.740.7676empty
2590.720.9827empty
310210.710.7697empty
4600.710.9825empty
56740.670.7655empty

Interfaces

1 interface between chains.

  • A–B · 240 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4N75 · Structural Basis of BamA-mediate Outer Membrane Protein Biogenesis · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A940 · AlphaFold monomer V2.0 prediction for outer membrane protein assembly factor bama (P0A940) · a predicted model of the same protein · chain A against A, TM-score 0.98

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