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NMR structure of escherichia COLI bame, a lipoprotein component of the beta-barrel assembly machinery complex

Analyse NMR structure of escherichia COLI bame, a lipoprotein component of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2KXX
Type
protein
Length
97 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Small protein a
UniProt
P0A937
Pockets
1 · best druggability 0.41

Structure

solution nmr · 1 distinct chain · 18% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASmall protein aprotein9718% helix, 22% strandP0A937

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11560.410.7329empty

Compared structures

  • 2KXX · NMR Structure of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A937 · AlphaFold monomer V2.0 prediction for outer membrane protein assembly factor bame (P0A937) · a predicted model of the same protein · chain A against A, TM-score 0.55

Analyse

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