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PDB | 1RX7 | STRUCTURE OF DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE

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Internal ID
21083
PDB Entry ID
1RX7
Title
STRUCTURE OF DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE
Authors
Primary Citation
AuthorsSawaya, M.R., Kraut, J.
TitleLoop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence.
JournalBiochemistry, v.36, pp.586 - 603, 1997
AbstractView
Pubmed9012674
DOI10.1021/bi962337c
 
History
Deposition: 1996-10-25Release: 1997-03-12Last Modified: 2009-02-24
Experimental Method
TypeX-RAY DIFFRACTION
Parameters
Resolution [Å]R-Value (Obs.)R-Value (Work)R-FreeSpace Group
2.30n/a0.181n/aP 21 21 21
Unit Cell
Length [Å]a34.99b45.31c101.14
Angles [°]alpha90.00beta90.00gamma90.00
Molecular Description
PolymerMoleculeMutationFragmentChainsEC NumberOther details
1DIHYDROFOLATE REDUCTASEA1.5.1.3
Functional Class
Source
PolymerScientific NameCommon NameExpression System
1Escherichia coliEscherichia coli
Chemical Component
IdentifierNameFormulaLigand StructureLigand Interaction
FOLFOLIC ACIDC19H19N7O6[View][View]
SCOP Classification
CATH Classification
Structural Details
KeywordOXIDOREDUCTASE
TextOXIDOREDUCTASE, NADP, TRIMETHOPRIM RESISTANCE, METHOTREXATE RESISTANCE, ONE-CARBON METABOLISM
 
Polymeric Molecules
Chain A
DescriptionDIHYDROFOLATE REDUCTASE
Polymer typepolypeptide
Formula Weight18020.5
Source Methodgenetically manipulated
Entity NameDHFR
Entity Name Sysn/a
 
Entity Poly
EntityChiralityLinkageMonomer# Mon.StrandTypeDetails
1n/anonon/aApolypeptide(L)n/a
Ligands And Prosthetic Groups
IDNameFormulaWeightLigand Structure
FOLFOLIC ACIDC19H19N7O6441.402View
EC and Associated Pathways
ChainsIUBMBKEGG EnzymeMetaCycReactome
A1.5.1.31.5.1.31.5.1.31.5.1.3
Natural/Genetically Modified Source
Scientific NameEscherichia coli
Source GenusEscherichia
Host Common Namen/a
Host Scientific NameEscherichia coli
Host GenusEscherichia coli
Host Cell Linen/a
Host Strainn/a
Host Vector Typen/a
Host PlasmidPRWA-1
 
Crystallization Experiments
Methodn/a
PH6.5
Temperaturen/a
DetailspH 6.5
 
Unit Cell
Length a (Å)Length b Å)Length c (Å)
34.9945.31101.14
Angle Alpha (°)Angle Beta (°)Angle Gamma (°)
90.0090.0090.00
Space Group
P 21 21 21
Diffraction Detector
DetectorAREA DETECTOR
TypeXUONG-HAMLIN MULTIWIRE
Detailsn/a
Collection Date1995-06
 
Diffraction Radiation
MonochromatorGRAPHITE(002)
Diffraction Protocoln/a
Wavelength1.5418
Wavelength Listn/a
 
Diffraction Source
SourceROTATING ANODE
TypeRIGAKU RUH2R
Siten/a
Beamlinen/a
 
Reflection Details
Observed Criterion Sigma (F)n/a
Observed Criterion Sigma (I)0.0
Resolution (High)2.30
Resolution (Low)100.00
Number Reflections (All) n/a
Number Reflections (Observed)6569
Percent Possible (Observed)87.0
R Merge I (Observed)n/a
Net I Over Average Sigma (I)n/a
B (Isotropic) From Wilson Plotn/a
Redundancy2.1
 
High Resolution Shell Details
Resolution(High)2.30
Resolution(Low)2.48
Percent Possible(All) 81.00
R Merge I(Observed)n/a
Mean I Over Sigma(Observed)2.1
R Sym I(Observed)0.175
Redundancy1.4
Num Unique Reflections(All)n/a
 
Refinement Statistics
Structure Solution MethodMOLECULAR REPLACEMENT
Resolution (High)2.30
Resolution (Low)20.00
Cut-off Sigma (F)0.0
Cut-off Sigma (I)n/a
Number of Reflections (All)n/a
Number of Reflections (Observed)6569
Number of Reflections (R-Free) n/a
Percent Reflections (Observed)87.00
R-Factor (All)n/a
R-Factor (Observed)n/a
R-Work0.181
R-Freen/a
R-Free Selection Detailsn/a
 
Temperature Factor Modeling
Isotropic Thermal Modeln/a
Mean Isotropic B Valuen/a
Anisotropic B[1][1]n/a
Anisotropic B[1][2]n/a
Anisotropic B[1][3]n/a
Anisotropic B[2][2]n/a
Anisotropic B[2][3]n/a
Anisotropic B[3][3]n/a
 
RMS Deviations
Parameter TypeDeviation From Ideal
t_bond_d0.022
t_angle_deg2.98
t_dihedral_angle_d25.0
t_incorr_chiral_ct0
t_pseud_anglen/a
t_trig_c_planes0.018
t_gen_planes0.006
t_it6.0
t_nbd0.017
Number of Non-Hydrogen Atoms Used in Refinement
Protein Atoms1268
Nucleic Acid Atoms0
Heterogen Atoms32
Solvent Atoms23
 
Programs
Data Collectionn/a
Data Reduction (intensity integration)UCSD
Data Reduction (data scaling)UCSD
Structure SolutionMERLOT
Structure RefinementTNT V. 5-D
 
Software
Classificationmodel building
Software NameMERLOT
 
Classificationrefinement
Software NameTNT
Software Version 5D
 
Sequence Chain
A
Sequence
  1   MISLIAALAV  DRVIGMENAM  PWNLPADLAW  FKRNTLDKPV  IMGRHTWESI  GRPLPGRKNI

 61   ILSSQPGTDD  RVTWVKSVDE  AIAACGDVPE  IMVIGGGRVY  EQFLPKAQKL  YLTHIDAEVE

121   GDTHFPDYEP  DDWESVFSEF  HDADAQNSHS  YCFEILERR