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- PDB-4tgl: CATALYSIS AT THE INTERFACE: THE ANATOMY OF A CONFORMATIONAL CHANG... -

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Basic information

Entry
Database: PDB / ID: 4tgl
TitleCATALYSIS AT THE INTERFACE: THE ANATOMY OF A CONFORMATIONAL CHANGE IN A TRIGLYCERIDE LIPASE
ComponentsTRIACYL-GLYCEROL ACYLHYDROLASE
KeywordsHYDROLASE(CARBOXYLIC ESTERASE)
Function / homology
Function and homology information


triacylglycerol lipase / triacylglycerol lipase activity / lipid catabolic process / metal ion binding
Similarity search - Function
: / 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
DIETHYL PHOSPHONATE / Lipase
Similarity search - Component
Biological speciesRhizomucor miehei (fungus)
MethodX-RAY DIFFRACTION / Resolution: 2.6 Å
AuthorsDerewenda, U. / Brzozowski, A.M. / Lawson, D. / Derewenda, Z.S.
Citation
Journal: Biochemistry / Year: 1992
Title: Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase.
Authors: Derewenda, U. / Brzozowski, A.M. / Lawson, D.M. / Derewenda, Z.S.
#1: Journal: To be Published
Title: Structure and Molecular Refinement of Rhizomucor Miehei Triacylglyceride Lipase: A Case Study of the Use of Simulated Annealing in Partial Model Refinement
Authors: Brzozowski, A.M. / Derewenda, Z.S. / Dodson, E.J. / Turkenburg, G.G.Dodson J.P.
#2: Journal: J.Mol.Biol. / Year: 1992
Title: The Crystal and Molecular Structure of the Rhizomucor Miehei Triacylglyceride Lipase at 1.9 Angstroms Resolution
Authors: Derewenda, Z.S. / Derewenda, U. / Dodson, G.G.
#3: Journal: Nature / Year: 1990
Title: A Serine Protease Triad Forms the Catalytic Centre of a Triacylglycerol Lipase
Authors: Brady, L. / Brzozowski, A.M. / Derewenda, Z.S. / Dodson, E. / Dodson, G. / Tolley, S. / Turkenburg, J.P. / Christiansen, L. / Huge-Jensen, B. / Norskov, L. / Thim, L. / Menge, U.
History
DepositionJul 29, 1991Processing site: BNL
Revision 1.0Jul 15, 1993Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jun 5, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_conn / 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 / _pdbx_database_status.process_site / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TRIACYL-GLYCEROL ACYLHYDROLASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,6612
Polymers29,5231
Non-polymers1381
Water4,288238
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)48.300, 93.900, 122.100
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Atom site foot note1: RESIDUES PRO 34, PRO 209, PRO 229, AND PRO 250 ARE CIS PROLINES.

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Components

#1: Protein TRIACYL-GLYCEROL ACYLHYDROLASE


Mass: 29522.969 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhizomucor miehei (fungus) / References: UniProt: P19515, triacylglycerol lipase
#2: Chemical ChemComp-DEP / DIETHYL PHOSPHONATE


Mass: 138.102 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H11O3P
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 238 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY
Sequence detailsRESIDUE 156 IN THIS ENTRY IS ASP AS IDENTIFIED BY ELECTRON DENSITY. IN THE CDNA SEQUENCE IT WAS ...RESIDUE 156 IN THIS ENTRY IS ASP AS IDENTIFIED BY ELECTRON DENSITY. IN THE CDNA SEQUENCE IT WAS INCORRECTLY ASSIGNED AS GLY.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.34 Å3/Da / Density % sol: 47.52 %
Crystal grow
*PLUS
Temperature: 37 ℃ / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
220 mg/mLprotein1drop
18-12 %PEG6001reservoir

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Data collection

Reflection
*PLUS
Highest resolution: 2.65 Å / Lowest resolution: 4.82 Å / Num. all: 8435 / Num. obs: 6017 / % possible obs: 74 % / Observed criterion σ(I): 2 / Redundancy: 3.6 % / Rmerge(I) obs: 0.1018

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Processing

SoftwareName: PROLSQ / Classification: refinement
RefinementRfactor obs: 0.129 / Highest resolution: 2.6 Å
Details: THERE ARE SOME ERRORS IN THE SEQUENCE DUE TO UNCERTAINTY IN THE ORIENTATION OF SIDE CHAINS. THESE DIFFERENCES ARE MINOR AND IN NO WAY COMPROMISE THE OVERALL QUALITY OF THE STRUCTURE OR THE ...Details: THERE ARE SOME ERRORS IN THE SEQUENCE DUE TO UNCERTAINTY IN THE ORIENTATION OF SIDE CHAINS. THESE DIFFERENCES ARE MINOR AND IN NO WAY COMPROMISE THE OVERALL QUALITY OF THE STRUCTURE OR THE SUITABILITY FOR MODELING OR MOLECULAR REPLACEMENT. SEQUENCE ADVISORY NOTICE: DIFFERENCE BETWEEN PIR AND PDB SEQUENCE. PIR ENTRY NAME: A34959 PIR RESIDUE PDB SEQRES NAME NUMBER NAME CHAIN SEQ/INSERT CODE ASP 181 ASN 181 GLU 220 SER 220
Refinement stepCycle: LAST / Highest resolution: 2.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2078 0 8 238 2324
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONp_bond_d0.0190.02
X-RAY DIFFRACTIONp_angle_d0.0690.04
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d0.0870.06
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it0.791
X-RAY DIFFRACTIONp_mcangle_it1.361.5
X-RAY DIFFRACTIONp_scbond_it1.61.5
X-RAY DIFFRACTIONp_scangle_it2.572
X-RAY DIFFRACTIONp_plane_restr0.0150.02
X-RAY DIFFRACTIONp_chiral_restr0.1590.12
X-RAY DIFFRACTIONp_singtor_nbd0.2340.5
X-RAY DIFFRACTIONp_multtor_nbd0.3250.5
X-RAY DIFFRACTIONp_xhyhbond_nbd
X-RAY DIFFRACTIONp_xyhbond_nbd
X-RAY DIFFRACTIONp_planar_tor2.633
X-RAY DIFFRACTIONp_staggered_tor23.775
X-RAY DIFFRACTIONp_orthonormal_tor33.715
X-RAY DIFFRACTIONp_transverse_tor
X-RAY DIFFRACTIONp_special_tor
Refinement
*PLUS
Highest resolution: 2.65 Å / Rfactor all: 0.146 / Lowest resolution: 10 Å / σ(I): 1
Solvent computation
*PLUS
Displacement parameters
*PLUS

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