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Crystal structure of a novel esterase CinB from Enterobacter asburiae

Analyse Crystal structure of a novel esterase CinB from Enterobacter asburiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6KMO
Type
protein
Length
658 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.45
Source
Enterobacter asburiae
Molecule
Alpha/beta hydrolase
UniProt
A0A1D3AXI2
Pockets
6 · best druggability 0.72

Structure

x-ray diffraction · resolution 1.45 · 2 distinct chains · 44% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha/beta hydrolaseprotein33044% helix, 21% strandA0A1D3AXI2
BAlpha/beta hydrolaseprotein32844% helix, 20% strandA0A1D3AXI2

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1710.720.9623empty
22130.620.8238empty
31770.490.7725empty
41680.470.7629empty
51550.450.7523empty

Interfaces

1 interface between chains.

  • A–B · 2490 Ų buried · 41 hydrogen bonds · protein-protein

Compared structures

  • 6KMO · Crystal structure of a novel esterase cinb from enterobacter asburiae · the same entry in another collection · chain A against A, TM-score 1.00

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