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Structure of E. COLI bama in complex with lipoprotein rcsf

Analyse Structure of E. COLI bama in complex with lipoprotein rcsf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6T1W
Type
protein
Length
1,388 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Outer membrane protein assembly factor bama; Outer membrane lipoprotein rcsf
UniProt
P0A940, E2QFC4
Pockets
20 · best druggability 0.88

Structure

x-ray diffraction · 4 distinct chains · 14% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOuter membrane protein assembly factor bamaprotein76115% helix, 42% strandP0A940
BOuter membrane protein assembly factor bamaprotein46610% helix, 48% strandP0A940
COuter membrane lipoprotein rcsfprotein8020% helix, 36% strandE2QFC4
DOuter membrane lipoprotein rcsfprotein8120% helix, 38% strandE2QFC4

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110500.880.90133empty
25890.860.9193empty
36360.800.8577empty
41550.780.9535empty
51130.780.9731empty

Interfaces

3 interfaces between chains.

  • A–C · 1771 Ų buried · 21 hydrogen bonds · protein-protein
  • B–D · 1618 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 529 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 6T1W · Structure of E. coli BamA in complex with lipoprotein RcsF · 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 B against A, TM-score 0.84

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