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- PDB-1cnf: STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE O... -

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Basic information

Entry
Database: PDB / ID: 1cnf
TitleSTRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE OF THE CYTOCHROME B REDUCTASE FRAGMENT AT 2.5 ANGSTROMS, ITS ADP COMPLEX AND AN ACTIVE SITE MUTANT AND MODELING OF THE CYTOCHROME B DOMAIN
ComponentsNITRATE REDUCTASE
KeywordsOXIDOREDUCTASE / NITROGENOUS ACCEPTOR / NITRATE ASSIMILATING ENZYME
Function / homology
Function and homology information


nitrate reductase (NADH) / nitrate reductase (NADH) activity / molybdenum ion binding / nitrate assimilation / nitric oxide biosynthetic process / FAD binding / heme binding / cytosol
Similarity search - Function
NADH:cytochrome b5 reductase-like / Moybdenum cofactor oxidoreductase, dimerisation / Mo-co oxidoreductase dimerisation domain / Eukaryotic molybdopterin oxidoreductase / Oxidoreductase molybdopterin binding domain / Oxidoreductase, molybdopterin-binding domain / Oxidoreductase, molybdopterin-binding domain superfamily / Oxidoreductase FAD-binding domain / Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain / Cytochrome b5 family, heme-binding domain signature. ...NADH:cytochrome b5 reductase-like / Moybdenum cofactor oxidoreductase, dimerisation / Mo-co oxidoreductase dimerisation domain / Eukaryotic molybdopterin oxidoreductase / Oxidoreductase molybdopterin binding domain / Oxidoreductase, molybdopterin-binding domain / Oxidoreductase, molybdopterin-binding domain superfamily / Oxidoreductase FAD-binding domain / Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain / Cytochrome b5 family, heme-binding domain signature. / Cytochrome b5, heme-binding site / Cytochrome b5 family, heme-binding domain profile. / Cytochrome b5-like heme/steroid binding domain superfamily / Cytochrome b5-like heme/steroid binding domain / Cytochrome b5-like Heme/Steroid binding domain / Cytochrome b5-like Heme/Steroid binding domain / Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module / Translation factors / Flavoprotein pyridine nucleotide cytochrome reductase / Oxidoreductase FAD/NAD(P)-binding / Oxidoreductase NAD-binding domain / Ferredoxin reductase-type FAD binding domain profile. / FAD-binding domain, ferredoxin reductase-type / Ferredoxin-NADP reductase (FNR), nucleotide-binding domain / Riboflavin synthase-like beta-barrel / Elongation Factor Tu (Ef-tu); domain 3 / Immunoglobulin E-set / Beta Barrel / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / FLAVIN-ADENINE DINUCLEOTIDE / Nitrate reductase [NADH]
Similarity search - Component
Biological speciesZea mays (maize)
MethodX-RAY DIFFRACTION / Resolution: 2.7 Å
AuthorsLu, G. / Lindqvist, Y. / Schneider, G.
Citation
Journal: J.Mol.Biol. / Year: 1995
Title: Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-site mutant and modeling of the cytochrome b domain.
Authors: Lu, G. / Lindqvist, Y. / Schneider, G. / Dwivedi, U. / Campbell, W.
#1: Journal: To be Published
Title: A Method for Processing Diffraction Data from Twinned Crystals and its Application in the Structure Determination of a Fad(Slash)Nadh Binding Fragment of Nitrate Reductase
Authors: Lu, G. / Lindqvist, Y. / Schneider, G.
#2: Journal: Structure / Year: 1995
Title: Crystal Structure of the Fad Containing Fragment of Corn Nitrate Reductase at 2.5 Angstroms Resolution: Relationship to Other Flavoprotein Reductase
Authors: Lu, G. / Campbell, W. / Lindqvist, Y. / Schneider, G.
#3: Journal: J.Mol.Biol. / Year: 1992
Title: Crystallization and Preliminary Crystallographic Studies of the Fad Domain of Corn Nadh:Nitrate Reductase
Authors: Lu, G. / Campbell, W. / Lindqvist, Y. / Schneider, G.
History
DepositionFeb 1, 1995-
Revision 1.0Apr 20, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: NITRATE REDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,8033
Polymers30,5901
Non-polymers1,2132
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)145.200, 145.200, 47.500
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number146
Space group name H-MH3
Atom site foot note1: CIS PROLINE - PRO 115 / 2: CIS PROLINE - PRO 163

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Components

#1: Protein NITRATE REDUCTASE /


Mass: 30590.322 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Zea mays (maize) / Organ: LEAF / References: UniProt: P17571, EC: 1.6.6.1
#2: Chemical ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE / Flavin adenine dinucleotide


Mass: 785.550 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#3: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.15 Å3/Da / Density % sol: 60.93 %

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionNum. obs: 8225 / % possible obs: 81 % / Observed criterion σ(I): 1
Reflection
*PLUS
Highest resolution: 2.7 Å / Redundancy: 2.4 % / Num. measured all: 20157 / Rmerge(I) obs: 0.062

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
RefinementResolution: 2.7→8 Å / σ(F): 1
RfactorNum. reflection
Rfree0.272 -
Rwork0.186 -
obs0.186 8225
Displacement parametersBiso mean: 33 Å2
Refinement stepCycle: LAST / Resolution: 2.7→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2074 0 80 0 2154
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.014
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_deg2.2
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
Refinement
*PLUS
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_deg27.9
X-RAY DIFFRACTIONx_improper_angle_deg2.1

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