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- PDB-1ubx: STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE -

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Basic information

Entry
Database: PDB / ID: 1ubx
TitleSTRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE
ComponentsFARNESYL DIPHOSPHATE SYNTHASE
KeywordsTRANSFERASE / ISOPRENE BIOSYNTHESIS / CHOLESTEROL BIOSYNTHESIS
Function / homology
Function and homology information


geranyl diphosphate biosynthetic process / dimethylallyltranstransferase / (2E,6E)-farnesyl diphosphate synthase / farnesyl diphosphate biosynthetic process / dimethylallyltranstransferase activity / geranyltranstransferase activity / cholesterol biosynthetic process / metal ion binding / cytoplasm
Similarity search - Function
Farnesyl pyrophosphate synthase-like / Polyprenyl synthases signature 2. / Polyprenyl synthases signature 1. / Polyprenyl synthetase, conserved site / Polyprenyl synthetase / Polyprenyl synthetase / Farnesyl Diphosphate Synthase / Farnesyl Diphosphate Synthase / Isoprenoid synthase domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
FARNESYL DIPHOSPHATE / Farnesyl pyrophosphate synthase
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodX-RAY DIFFRACTION / Resolution: 2.5 Å
AuthorsTarshis, L.C. / Proteau, P. / Poulter, C.D. / Sacchettini, J.C.
Citation
Journal: Proc.Natl.Acad.Sci.USA / Year: 1996
Title: Regulation of product chain length by isoprenyl diphosphate synthases.
Authors: Tarshis, L.C. / Proteau, P.J. / Kellogg, B.A. / Sacchettini, J.C. / Poulter, C.D.
#1: Journal: Biochemistry / Year: 1994
Title: Crystal Structure of Recombinant Farnesyl Diphosphate Synthase at 2.6-A Resolution
Authors: Tarshis, L.C. / Yan, M. / Poulter, C.D. / Sacchettini, J.C.
History
DepositionOct 14, 1996Processing site: BNL
Revision 1.0Mar 12, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Feb 14, 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.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _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: FARNESYL DIPHOSPHATE SYNTHASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,4783
Polymers42,0711
Non-polymers4072
Water81145
1
A: FARNESYL DIPHOSPHATE SYNTHASE
hetero molecules

A: FARNESYL DIPHOSPHATE SYNTHASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,9556
Polymers84,1422
Non-polymers8134
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation10_565-x,-y+1,z1
Buried area6440 Å2
ΔGint-49 kcal/mol
Surface area30380 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)88.700, 88.700, 276.300
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number98
Space group name H-MI4122

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Components

#1: Protein FARNESYL DIPHOSPHATE SYNTHASE / FPS


Mass: 42071.105 Da / Num. of mol.: 1 / Mutation: F112A, F113S
Source method: isolated from a genetically manipulated source
Details: COMPLEXED WITH FARNESYL DIPHOSPHATE AND MAGNESIUM / Source: (gene. exp.) Gallus gallus (chicken) / Organ: LIVER / Plasmid: PUC / Production host: Escherichia coli (E. coli) / References: UniProt: P08836, dimethylallyltranstransferase
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-FPP / FARNESYL DIPHOSPHATE


Mass: 382.326 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C15H28O7P2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 45 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.23 Å3/Da / Density % sol: 61.9 %
Crystal grow
*PLUS
pH: 7 / Method: unknown
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
112 %PEG600011
21.3 M11NaCl
330 mMBHDA11
45 mMmagnesium11
516-20 mg/mlFPS11

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Data collection

Diffraction sourceWavelength: 1.5418
DetectorType: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR / Date: Aug 18, 1995
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionNum. obs: 19491 / % possible obs: 86 % / Observed criterion σ(I): 0.2 / Redundancy: 2.9 % / Rmerge(I) obs: 0.06

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Processing

Software
NameVersionClassification
TNT5Erefinement
SADIEdata reduction
RefinementHighest resolution: 2.5 Å / Num. reflection obs: 16544 / σ(F): 2
Refinement stepCycle: LAST / Highest resolution: 2.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2804 0 25 45 2874
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONt_bond_d0.02
X-RAY DIFFRACTIONt_angle_deg2.54
X-RAY DIFFRACTIONt_dihedral_angle_d
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes
X-RAY DIFFRACTIONt_it
X-RAY DIFFRACTIONt_nbd

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