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Refined crystal structure of beta-lactamase from citrobacter freundii indicates a mechanism for beta-lactam hydrolysis

Analyse Refined crystal structure of beta-lactamase from citrobacter freundii indicates… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FR1
Type
protein
Length
722 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-lactamase
EC
3.5.2.6
UniProt
Q46041
Pockets
5 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BBeta-lactamase (EC 3.5.2.6)protein36140% helix, 24% strandQ46041

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18670.870.90104empty
23870.770.8753empty
31060.380.7520empty
4530.360.8015empty
5600.310.7618empty

Interfaces

1 interface between chains.

  • A–B · 1476 Ų buried · 21 hydrogen bonds · protein-protein

Compared structures

  • 1FR1 · Refined crystal structure of beta-lactamase from citrobacter freundii indicates a… · the same entry in another collection · chain A against A, TM-score 1.00

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