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- PDB-7dtn: Crystal structure of metallo-beta-lactamase IMP-1 mutant (D120E) ... -

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Basic information

Entry
Database: PDB / ID: 7dtn
TitleCrystal structure of metallo-beta-lactamase IMP-1 mutant (D120E) in complex with citrate.
ComponentsMetallo-beta-lactamase type 2
KeywordsHYDROLASE / metallo-beta-lactamase / zinc(II) ion / citrate
Function / homology
Function and homology information


antibiotic catabolic process / beta-lactamase activity / beta-lactamase / periplasmic space / response to antibiotic / zinc ion binding
Similarity search - Function
Beta-lactamases class B signature 2. / Beta-lactamases class B signature 1. / Beta-lactamase, class-B, conserved site / : / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase / Ribonuclease Z/Hydroxyacylglutathione hydrolase-like
Similarity search - Domain/homology
2-(2-ETHOXYETHOXY)ETHANOL / CITRATE ANION / Metallo-beta-lactamase type 2
Similarity search - Component
Biological speciesSerratia marcescens (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.85 Å
AuthorsYamaguchi, Y. / Kurosaki, H.
Funding support Japan, 2items
OrganizationGrant numberCountry
Japan Agency for Medical Research and Development (AMED) Japan
Japan Society for the Promotion of Science (JSPS) Japan
CitationJournal: J.Med.Chem. / Year: 2021
Title: Crystal Structures of Metallo-beta-Lactamase (IMP-1) and Its D120E Mutant in Complexes with Citrate and the Inhibitory Effect of the Benzyl Group in Citrate Monobenzyl Ester.
Authors: Yamaguchi, Y. / Kato, K. / Ichimaru, Y. / Jin, W. / Sakai, M. / Abe, M. / Wachino, J.I. / Arakawa, Y. / Miyagi, Y. / Imai, M. / Fukuishi, N. / Yamagata, Y. / Otsuka, M. / Fujita, M. / Kurosaki, H.
History
DepositionJan 6, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 4, 2021Provider: repository / Type: Initial release
Revision 1.1Nov 29, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Metallo-beta-lactamase type 2
B: Metallo-beta-lactamase type 2
C: Metallo-beta-lactamase type 2
D: Metallo-beta-lactamase type 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)102,65120
Polymers100,8354
Non-polymers1,81616
Water11,295627
1
A: Metallo-beta-lactamase type 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,6635
Polymers25,2091
Non-polymers4544
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area630 Å2
ΔGint-78 kcal/mol
Surface area10020 Å2
MethodPISA
2
B: Metallo-beta-lactamase type 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,6635
Polymers25,2091
Non-polymers4544
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area630 Å2
ΔGint-78 kcal/mol
Surface area9910 Å2
MethodPISA
3
C: Metallo-beta-lactamase type 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,6635
Polymers25,2091
Non-polymers4544
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area630 Å2
ΔGint-78 kcal/mol
Surface area9970 Å2
MethodPISA
4
D: Metallo-beta-lactamase type 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,6635
Polymers25,2091
Non-polymers4544
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area630 Å2
ΔGint-78 kcal/mol
Surface area9810 Å2
MethodPISA
Unit cell
Length a, b, c (Å)49.709, 72.862, 82.188
Angle α, β, γ (deg.)84.780, 75.580, 73.690
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
Metallo-beta-lactamase type 2 / B2 metallo-beta-lactamase / BLA-IMP / IMP-1 / Beta-lactamase type II / Metallo-beta-lactamase type II


Mass: 25208.699 Da / Num. of mol.: 4 / Mutation: D81E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Serratia marcescens (bacteria) / Plasmid: pET9a / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P52699, beta-lactamase
#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-FLC / CITRATE ANION


Mass: 189.100 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H5O7 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-AE3 / 2-(2-ETHOXYETHOXY)ETHANOL


Mass: 134.174 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H14O3
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 627 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.74 Å3/Da / Density % sol: 55.16 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 0.1M citric acid-sodium citrate buffer, 0.2M sodium acetate, PEG4000 30 w/v%

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-5A / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 16, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.85→50 Å / Num. obs: 89488 / % possible obs: 97.7 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 26.4
Reflection shellResolution: 1.85→1.88 Å / Rmerge(I) obs: 0.332 / Mean I/σ(I) obs: 5 / Num. unique obs: 4327

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Processing

Software
NameVersionClassification
REFMAC5.7.0032refinement
PDB_EXTRACT3.27data extraction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1dd6

1dd6


Resolution: 1.85→30 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.943 / SU B: 2.287 / SU ML: 0.07 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.116 / ESU R Free: 0.111 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.1963 4481 5 %RANDOM
Rwork0.1635 ---
obs0.1651 85006 97.49 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 70.04 Å2 / Biso mean: 19.461 Å2 / Biso min: 8.68 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å2-0 Å2
2---0 Å2-0 Å2
3---0 Å2
Refinement stepCycle: final / Resolution: 1.85→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6828 0 96 627 7551
Biso mean--30.87 25.22 -
Num. residues----872
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0197135
X-RAY DIFFRACTIONr_bond_other_d0.0010.026857
X-RAY DIFFRACTIONr_angle_refined_deg1.3751.9779690
X-RAY DIFFRACTIONr_angle_other_deg0.73315899
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9815882
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.98225.106282
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.747151217
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.1981513
X-RAY DIFFRACTIONr_chiral_restr0.0780.21071
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0217878
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021515
LS refinement shellResolution: 1.85→1.896 Å / Rfactor Rfree error: 0
RfactorNum. reflection% reflection
Rfree0.254 302 -
Rwork0.225 5969 -
obs--93.11 %

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