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Crystal structure of the kpc-2 beta-lactamase complexed with hydrolyzed cefotaxime

Analyse Crystal structure of the kpc-2 beta-lactamase complexed with hydrolyzed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5UJ3
Type
protein
Length
269 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Carbapenem-hydrolyzing beta-lactamase kpc
EC
3.5.2.6
UniProt
Q9F663
Ligands
CE4

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACarbapenem-hydrolyzing beta-lactamase kpc (EC 3.5.2.6)protein26944% helix, 17% strandQ9F663

Ligands and binding sites

  • CE4 · (2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-methylidene-5,6-dihydro -2H-1,3-thiazine-4-carboxylic acid · ligand · 2 copies · chains A
  • GOL · Glycerol · additive · chains A

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

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 5UJ3 · Crystal structure of the KPC-2 beta-lactamase complexed with hydrolyzed cefotaxime · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9F663 · AlphaFold monomer V2.0 prediction for carbapenem-hydrolyzing beta- lactamase kpc (Q9F663) · a predicted model of the same protein · chain A against A, TM-score 0.98

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