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- PDB-1cet: CHLOROQUINE BINDS IN THE COFACTOR BINDING SITE OF PLASMODIUM FALC... -

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Basic information

Entry
Database: PDB / ID: 1cet
TitleCHLOROQUINE BINDS IN THE COFACTOR BINDING SITE OF PLASMODIUM FALCIPARUM LACTATE DEHYDROGENASE.
ComponentsPROTEIN (L-LACTATE DEHYDROGENASE)
KeywordsOXIDOREDUCTASE / TRICARBOXYLIC ACID CYCLE / INHIBITOR
Function / homology
Function and homology information


L-lactate dehydrogenase / L-lactate dehydrogenase (NAD+) activity / lactate metabolic process / pyruvate metabolic process
Similarity search - Function
Malate dehydrogenase, type 3 / L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2 / Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal / L-lactate/malate dehydrogenase / Lactate/malate dehydrogenase, N-terminal / Lactate/malate dehydrogenase, C-terminal / lactate/malate dehydrogenase, NAD binding domain / lactate/malate dehydrogenase, alpha/beta C-terminal domain / Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal / NAD(P)-binding Rossmann-like Domain ...Malate dehydrogenase, type 3 / L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2 / Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal / L-lactate/malate dehydrogenase / Lactate/malate dehydrogenase, N-terminal / Lactate/malate dehydrogenase, C-terminal / lactate/malate dehydrogenase, NAD binding domain / lactate/malate dehydrogenase, alpha/beta C-terminal domain / Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Alpha-Beta Complex / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-CLQ / L-lactate dehydrogenase
Similarity search - Component
Biological speciesPlasmodium falciparum (malaria parasite P. falciparum)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.05 Å
AuthorsRead, J.A. / Wilkinson, K.W. / Tranter, R. / Sessions, R.B. / Brady, R.L.
Citation
Journal: J.Biol.Chem. / Year: 1999
Title: Chloroquine binds in the cofactor binding site of Plasmodium falciparum lactate dehydrogenase.
Authors: Read, J.A. / Wilkinson, K.W. / Tranter, R. / Sessions, R.B. / Brady, R.L.
#1: Journal: Nat.Struct.Biol. / Year: 1996
Title: The Structure of Lactate Dehydrogenase from Plasmodium Falciparum Reveals a New Target for Anti-Malarial Design
Authors: Dunn, C.R. / Banfield, M.J. / Barker, J.J. / Higham, C.W. / Moreton, K.M. / Turgut-Balik, D. / Brady, R.L. / Holbrook, J.J.
History
DepositionMar 10, 1999Deposition site: PDBE / Processing site: RCSB
Revision 1.0Mar 19, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Aug 9, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PROTEIN (L-LACTATE DEHYDROGENASE)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,4832
Polymers34,1631
Non-polymers3201
Water4,540252
1
A: PROTEIN (L-LACTATE DEHYDROGENASE)
hetero molecules

A: PROTEIN (L-LACTATE DEHYDROGENASE)
hetero molecules

A: PROTEIN (L-LACTATE DEHYDROGENASE)
hetero molecules

A: PROTEIN (L-LACTATE DEHYDROGENASE)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,9318
Polymers136,6514
Non-polymers1,2794
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-x+1,-y+1,z1
crystal symmetry operation3_655-x+1,y,-z1
crystal symmetry operation4_565x,-y+1,-z1
Buried area16970 Å2
ΔGint-118 kcal/mol
Surface area40950 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)79.930, 85.440, 92.190
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222

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Components

#1: Protein PROTEIN (L-LACTATE DEHYDROGENASE)


Mass: 34162.785 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum)
Plasmid: PKK223-3 / Production host: Escherichia coli (E. coli) / References: UniProt: Q27743, L-lactate dehydrogenase
#2: Chemical ChemComp-CLQ / N4-(7-CHLORO-QUINOLIN-4-YL)-N1,N1-DIETHYL-PENTANE-1,4-DIAMINE / CHLOROQUINE


Mass: 319.872 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H26ClN3 / Comment: medication, antiparasitic*YM
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 252 / Source method: isolated from a natural source / Formula: H2O

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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: 2.3 Å3/Da / Density % sol: 40 %
Crystal growpH: 7.5 / Details: pH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SRS / Beamline: PX7.2 / Wavelength: 1.488
DetectorType: MARRESEARCH / Detector: IMAGE PLATE
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.488 Å / Relative weight: 1
ReflectionResolution: 2.05→20 Å / Num. obs: 20155 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 2.3 % / Rmerge(I) obs: 0.067 / Net I/σ(I): 16.3

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
X-PLOR3.851refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1LDG

1ldg


Resolution: 2.05→20 Å / Data cutoff high absF: 20 / Data cutoff low absF: 2.05 / Cross valid method: THROUGHOUT / σ(F): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.193 -5 %RANDOM
Rwork0.154 ---
obs-20115 99.8 %-
Displacement parametersBiso mean: 9.1 Å2
Refinement stepCycle: LAST / Resolution: 2.05→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2305 0 22 252 2579
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.006
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg0.023
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Software
*PLUS
Name: X-PLOR / Version: 3.851 / Classification: refinement
Refinement
*PLUS
Num. reflection all: 20115 / Num. reflection obs: 17783
Solvent computation
*PLUS
Displacement parameters
*PLUS

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