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Cryo-EM structure of the nitrilase from pseudomonas fluorescens EBC191 at 3.3 ångströms

Analyse Cryo-EM structure of the nitrilase from pseudomonas fluorescens EBC191 at 3.3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZBY
Type
protein
Length
3,792 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nita
UniProt
Q5EG61
Pockets
20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 30% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LNitaprotein31630% helix, 26% strandQ5EG61

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12100.810.9559empty
210100.810.82113empty
33610.800.9080empty
42280.790.9258empty
52030.780.9259empty

Interfaces

25 interfaces between chains.

  • B–C · 2584 Ų buried · 31 hydrogen bonds · protein-protein
  • J–K · 2529 Ų buried · 34 hydrogen bonds · protein-protein
  • D–E · 2517 Ų buried · 34 hydrogen bonds · protein-protein
  • H–I · 2505 Ų buried · 30 hydrogen bonds · protein-protein
  • F–G · 2493 Ų buried · 31 hydrogen bonds · protein-protein

Compared structures

  • 6ZBY · Cryo-EM structure of the nitrilase from Pseudomonas fluorescens EBC191 at 3.3 Angstroms · the same entry in another collection · chain A against A, TM-score 1.00

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