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MolNFT v2 · #119912 · protein

Direct Observation of Active-site Protonation States in a Class A beta lactamase with a monobactam substrate

5G18: “Direct Observation of Active-site Protonation States in a Class A beta lactamase with a monobactam substrate”. X-ray diffraction at 1.1, 2 ligands (AZR, SO4). MolNFT v2 #119912 on GenesisL1: 3D structure, binding sites and pockets…

PDB
5G18
Type
protein
Length
261 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.1
Source
ESCHERICHIA COLI
UniProt
E1ANH6
Ligands
AZR, SO4

Structure

x-ray diffraction · resolution 1.1 · 1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein261—E1ANH6

Ligands and binding sites

  • AZR · 2-({[(1Z)-1-(2-amino-1,3-thiazol-4-yl)-2-oxo-2-{[(2S, 3S)-1-oxo-3-(sulfoamino)butan-2-yl]amino}ethylidene]amino}oxy)-2-methylpropanoic acid · ligand · chains A
  • SO4 · Sulfate ion · ion · 5 copies · chains A

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

Compared structures

  • 5G18 · Direct observation of active-site protonation states in a class a beta lactamase with a… · the same entry in another collection · chain A against A, TM-score 1.00
  • E1ANH6 · AlphaFold monomer V2.0 prediction for beta-lactamase ctx-M-97 (E1ANH6) · a predicted model of the same protein · chain A against A, TM-score 0.99

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