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Nora in complex with FAB36

Analyse Nora in complex with FAB36 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LO8
Type
protein
Length
815 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Quinolone resistance protein nora; FAB36 heavy chain; FAB36 light chain
UniProt
Q53459
Pockets
10 · best druggability 0.84

Structure

electron microscopy · 3 distinct chains · 38% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ZQuinolone resistance protein noraprotein36978% helix, 0% strandQ53459
HFAB36 heavy chainprotein2317% helix, 38% strand—
LFAB36 light chainprotein2154% helix, 40% strand—

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12610.840.9535empty
22450.660.8352empty
34050.580.7556empty
41020.420.7822empty
5610.410.8114empty

Interfaces

3 interfaces between chains.

  • H–L · 2147 Ų buried · 17 hydrogen bonds · protein-protein
  • Z–H · 1535 Ų buried · 13 hydrogen bonds · protein-protein
  • Z–L · 977 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 7LO8 · NorA in complex with Fab36 · the same entry in another collection · chain Z against Z, TM-score 1.00

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