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Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (apo form)

Analyse Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (apo form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FU6
Type
protein
Length
532 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Metallo-beta-lactamase L1
EC
3.5.2.6
UniProt
P52700
Ligands
SO4
Pockets
4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMetallo-beta-lactamase L1 (EC 3.5.2.6)protein26630% helix, 24% strandP52700

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 8 copies · chains A, B
  • GOL · Glycerol · additive · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12270.630.8237empty
21200.420.7627empty
31040.400.7626empty
4580.280.7411GOL

Interfaces

1 interface between chains.

  • A–B · 1328 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 2FU6 · Zinc-beta-lactamase l1 from stenotrophomonas maltophilia (apo form) · the same entry in another collection · chain A against A, TM-score 1.00
  • P52700 · AlphaFold monomer V2.0 prediction for metallo-beta-lactamase L1 type 3 (P52700) · a predicted model of the same protein · chain B against A, TM-score 1.00

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