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- PDB-1gao: CRYSTAL STRUCTURE OF THE L44S MUTANT OF FERREDOXIN I -

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Basic information

Entry
Database: PDB / ID: 1gao
TitleCRYSTAL STRUCTURE OF THE L44S MUTANT OF FERREDOXIN I
ComponentsFERREDOXIN I
KeywordsELECTRON TRANSPORT / Iron-sulfur clusters / ferredoxin
Function / homology
Function and homology information


3 iron, 4 sulfur cluster binding / 4 iron, 4 sulfur cluster binding / electron transfer activity / DNA binding / metal ion binding
Similarity search - Function
Ferredoxin, C-terminal / : / Domain of unknown function (DUF3470) / 7Fe ferredoxin / : / Alpha-Beta Plaits - #20 / 4Fe-4S binding domain / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. ...Ferredoxin, C-terminal / : / Domain of unknown function (DUF3470) / 7Fe ferredoxin / : / Alpha-Beta Plaits - #20 / 4Fe-4S binding domain / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
FE3-S4 CLUSTER / IRON/SULFUR CLUSTER / Ferredoxin-1
Similarity search - Component
Biological speciesAzotobacter vinelandii (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsStout, C.D. / Burgess, B.K. / Prasad, G.S. / Sridhar, V. / Jung, Y.S.
CitationJournal: J.Biol.Chem. / Year: 2002
Title: Azotobacter vinelandii ferredoxin I: a sequence and structure comparison approach to alteration of [4Fe-4S]2+/+ reduction potential.
Authors: Chen, K. / Jung, Y.S. / Bonagura, C.A. / Tilley, G.J. / Prasad, G.S. / Sridhar, V. / Armstrong, F.A. / Stout, C.D. / Burgess, B.K.
History
DepositionNov 30, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 13, 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 1.4Oct 27, 2021Group: Database references / Derived calculations / Category: database_2 / 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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Aug 9, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: FERREDOXIN I
B: FERREDOXIN I
C: FERREDOXIN I
D: FERREDOXIN I
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,72412
Polymers48,1344
Non-polymers2,5908
Water4,630257
1
A: FERREDOXIN I
hetero molecules


Theoretical massNumber of molelcules
Total (without water)12,6813
Polymers12,0331
Non-polymers6472
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: FERREDOXIN I
hetero molecules


Theoretical massNumber of molelcules
Total (without water)12,6813
Polymers12,0331
Non-polymers6472
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: FERREDOXIN I
hetero molecules


Theoretical massNumber of molelcules
Total (without water)12,6813
Polymers12,0331
Non-polymers6472
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: FERREDOXIN I
hetero molecules


Theoretical massNumber of molelcules
Total (without water)12,6813
Polymers12,0331
Non-polymers6472
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)130.8, 85.6, 67.2
Angle α, β, γ (deg.)90.0, 117.9, 90.0
Int Tables number5
Space group name H-MC121

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Components

#1: Protein
FERREDOXIN I


Mass: 12033.450 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Azotobacter vinelandii (bacteria) / References: UniProt: P00214
#2: Chemical
ChemComp-SF4 / IRON/SULFUR CLUSTER


Mass: 351.640 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe4S4
#3: Chemical
ChemComp-F3S / FE3-S4 CLUSTER


Mass: 295.795 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe3S4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 257 / Source method: isolated from a natural source / Formula: H2O

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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: 3.45 Å3/Da / Density % sol: 64.36 %
Crystal growTemperature: 277 K / Method: vapor diffusion / pH: 7.5
Details: Ammonium sulfate, Lithium sulfate, Tris buffer, pH 7.5, VAPOR DIFFUSION, temperature 277K
Crystal grow
*PLUS
Temperature: 2 ℃ / pH: 7.4 / Details: Shen, B., (1994) J. Biol. Chem., 269, 8564.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
17-10 mg/mlprotein1drop
20.5 Mpotassium phosphate1drop
31.2 Mammonium sulfate1drop
43.5 Mammonium sulfate1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.08 Å
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 17, 2000 / Details: SSRL beam line 7-1
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.08 Å / Relative weight: 1
ReflectionResolution: 2.2→50 Å / Num. all: 55252 / Num. obs: 30964 / % possible obs: 93.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 1.8 % / Rmerge(I) obs: 0.136

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Processing

Software
NameVersionClassification
MAR345data collection
MOSFLMdata reduction
AMoREphasing
X-PLOR3.851refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7FD1

7fd1


Resolution: 2.2→50 Å / Isotropic thermal model: Isotropic / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Xplor3.8
RfactorNum. reflectionSelection details
Rfree0.286 928 3% of data
Rwork0.243 --
all0.243 30964 -
obs0.243 30953 -
Displacement parametersBiso mean: 44.4 Å2
Refinement stepCycle: LAST / Resolution: 2.2→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3356 0 60 257 3673
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.015
X-RAY DIFFRACTIONc_angle_deg2.7
Software
*PLUS
Name: X-PLOR / Version: 3.851 / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDType
X-RAY DIFFRACTIONx_bond_d
X-RAY DIFFRACTIONx_angle_deg

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