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- PDB-1ein: THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (... -

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Basic information

Entry
Database: PDB / ID: 1ein
TitleTHE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE
ComponentsLIPASE
KeywordsHYDROLASE / alpha-beta structure
Function / homology
Function and homology information


triacylglycerol lipase / triacylglycerol lipase activity / lipid catabolic process
Similarity search - Function
Mono-/di-acylglycerol lipase, N-terminal / Lipase 3 N-terminal region / : / Fungal lipase-like domain / Lipase (class 3) / Lipases, serine active site. / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
DIUNDECYL PHOSPHATIDYL CHOLINE / Lipase
Similarity search - Component
Biological speciesThermomyces lanuginosus (fungus)
MethodX-RAY DIFFRACTION / Resolution: 3 Å
AuthorsBrozozowski, A.M. / Savage, H.
CitationJournal: Biochemistry / Year: 2000
Title: Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase.
Authors: Brzozowski, A.M. / Savage, H. / Verma, C.S. / Turkenburg, J.P. / Lawson, D.M. / Svendsen, A. / Patkar, S.
History
DepositionFeb 26, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 20, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 4, 2017Group: Refinement description / Category: software
Revision 1.4Jan 31, 2018Group: Experimental preparation / Category: exptl_crystal_grow
Item: _exptl_crystal_grow.pdbx_details / _exptl_crystal_grow.temp
Revision 1.5Oct 16, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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: LIPASE
B: LIPASE
C: LIPASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,8966
Polymers88,0273
Non-polymers1,8693
Water3,315184
1
A: LIPASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,9652
Polymers29,3421
Non-polymers6231
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: LIPASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,9652
Polymers29,3421
Non-polymers6231
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: LIPASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,9652
Polymers29,3421
Non-polymers6231
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)135.950, 135.950, 149.990
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number170
Space group name H-MP65
DetailsThe biological assembly is a monomer

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Components

#1: Protein LIPASE


Mass: 29342.484 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Thermomyces lanuginosus (fungus) / References: UniProt: O59952, triacylglycerol lipase
#2: Chemical ChemComp-PLC / DIUNDECYL PHOSPHATIDYL CHOLINE


Mass: 622.834 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C32H65NO8P / Comment: phospholipid*YM
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 184 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 4.54 Å3/Da / Density % sol: 72.93 %
Crystal growMethod: vapor diffusion, hanging drop / pH: 8.1
Details: PEG 5000, magnesium chloride, c8e5 , pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 110K
Crystal grow
*PLUS
Method: unknown
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
15 mg/mlprotein1drop
210 mMTris-HCl1drop
30.1 MTris-HCl1reservoir
425 mM1reservoirMgCl2
517 %(w/v)mPEG50001reservoir

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.54
DetectorType: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Jun 1, 1996
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 3→27.4 Å / Num. all: 91965 / Num. obs: 31460 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.2 % / Rmerge(I) obs: 0.2 / Net I/σ(I): 3
Reflection shellResolution: 3→3.16 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.139 / Num. unique all: 31460 / % possible all: 100
Reflection
*PLUS
% possible obs: 99.5 %
Reflection shell
*PLUS
% possible obs: 98.2 % / Redundancy: 2.1 % / Rmerge(I) obs: 0.425 / Mean I/σ(I) obs: 1.8

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Processing

Software
NameVersionClassification
ROTAVATAdata reduction
AMoREphasing
REFMACrefinement
CCP4(AGROVATAdata scaling
ROTAVATAdata scaling
RefinementResolution: 3→27.4 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber / Details: R-axis data
RfactorNum. reflection% reflectionSelection details
Rfree0.241 1588 -random
Rwork0.21 ---
all-164254 --
obs-31460 99.8 %-
Refinement stepCycle: LAST / Resolution: 3→27.4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6189 0 126 184 6499
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_bond_d0.008
X-RAY DIFFRACTIONo_angle_deg0.029
Software
*PLUS
Name: REFMAC / Classification: refinement
Refinement
*PLUS
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 34.1 Å2
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONp_bond_d
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_plane_restr0.029

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