3S22

AMP-C BETA-LACTAMASE (PSEUDOMONAS AERUGINOSA) in complex with an inhibitor

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.219 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.184 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history. 


Literature

Side chain SAR of bicyclic Beta-lactamase inhibitors (BLIs). 2. N-Alkylated and open chain analogs of MK-8712

Chen, H., Blizzard, T.A., Kim, S., Wu, J., Young, K., Park, Y.W., Ogawa, A.M., Raghoobar, S., Painter, R.E., Wisniewski, D., Hairston, N., Fitzgerald, P., Sharma, N., Scapin, G., Lu, J., Hermes, J., Hammond, M.L.

(2011) Bioorg Med Chem Lett 21: 4267-4270

  • DOI: https://doi.org/10.1016/j.bmcl.2011.05.065
  • Primary Citation of Related Structures:  
    3S1Y, 3S22

  • PubMed Abstract: 

    The bridged monobactam β-lactamase inhibitor MK-8712 (1) effectively inhibits class C β-lactamases. Side chain N-alkylated and ring-opened analogs of 1 were prepared and evaluated for combination with imipenem to overcome class C β-lactamase mediated resistance. Although some analogs were more potent inhibitors of AmpC, none exhibited better synergy with imipenem than 1.

    • Organizational Affiliation: 

    Departments of Medicinal Chemistry, Merck Research Labs, Rahway, NJ 07065, USA. [email protected]


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-lactamase371Pseudomonas aeruginosaMutation(s): 1 
Gene Names: ampC, PA4110
EC: 3.5.2.6
UniProt
Find proteins for P24735 (Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1))
Explore P24735 
Go to UniProtKB:  P24735
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP24735
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
3S2
Query on 3S2
Download Ideal Coordinates CCD File 
B [auth A][(2S,3R)-2-formyl-1-{[4-(methylamino)butyl]carbamoyl}pyrrolidin-3-yl]sulfamic acid
C11 H22 N4 O5 S
KICDPLXBZKSLNF-NXEZZACHSA-N
CL
Query on CL
Download Ideal Coordinates CCD File 
C [auth A]CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Binding Affinity Annotations 
IDSourceBinding Affinity
3S2 PDBBind:  3S22 IC50: 3500 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.219 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.184 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 44.891α = 90
b = 71.891β = 90
c = 105.889γ = 90
Software Package:
Software NamePurpose
StructureStudiodata collection
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
REFMACphasing

Structure Validation

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Ligand Structure Quality Assessment 


View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-06-29
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2013-06-26
    Changes: Database references
  • Version 1.3: 2024-10-30
    Changes: Data collection, Database references, Derived calculations, Structure summary