1FCN

Crystal Structure of the E. Coli AMPC Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Substrate Beta-Lactam LORACARBEF

PDB DOI: https://doi.org/10.2210/pdb1FCN/pdb

Classification: HYDROLASE
Organism(s): Escherichia coli
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2000-07-18 Released: 2000-12-04
Deposition Author(s): Patera, A., Blaszczak, L.C., Shoichet, B.K.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.35 Å
R-Value Free: 0.257
R-Value Work: 0.208

wwPDB Validation 3D Report Full Report

This is version 1.6 of the entry. See complete history.

Literature

Crystal Structures of Substrate and Inhibitor Complexes with AmpC -Lactamase: Possible Implications for Substrate-Assisted Catalysis

Patera, A., Blaszczak, L.C., Shoichet, B.K.

(2000) J Am Chem Soc 122: 10504-10512

DOI: https://doi.org/10.1021/ja001676x

Macromolecule Content

Total Structure Weight: 79.78 kDa
Atom Count: 5,715
Modelled Residue Count: 710
Deposited Residue Count: 716
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
BETA-LACTAMASE	A, B	358	Escherichia coli	Mutation(s): 2 EC: 3.5.2.6
UniProt
Find proteins for P00811 (Escherichia coli (strain K12)) Explore P00811 Go to UniProtKB: P00811
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P00811
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
LOR Query on LOR Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth B]	C [auth A], D [auth B]	LORACABEF (Open form) C₁₆ H₁₈ Cl N₃ O₄ DRTWKGBDHBOYMS-UMSGYPCISA-N		Interactions Focus chain C [auth A] Focus chain D [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.35 Å
R-Value Free: 0.257
R-Value Work: 0.208
Space Group: C 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 119.36	α = 90
b = 76.264	β = 116
c = 98.355	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
SCALEPACK	data scaling
CNS	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2000-12-04

Deposition Author(s):

Blaszczak, L.C.

Revision History (Full details and data files)

Version 1.0: 2000-12-04
Type: Initial release
Version 1.1: 2007-10-21
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2011-08-24
Changes: Non-polymer description
Version 1.4: 2017-10-04
Changes: Refinement description
Version 1.5: 2018-02-14
Changes: Experimental preparation
Version 1.6: 2021-11-03
Changes: Database references, Derived calculations

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.