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- PDB-1byp: E43K,D44K DOUBLE MUTANT PLASTOCYANIN FROM SILENE -

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Basic information

Entry
Database: PDB / ID: 1byp
TitleE43K,D44K DOUBLE MUTANT PLASTOCYANIN FROM SILENE
ComponentsPROTEIN (PLASTOCYANIN)
KeywordsELECTRON TRANSPORT / ELECTRON TRANSFER / PHOTOSYNTHESIS / ACIDIC PATCH / DOUBLE MUTANT
Function / homology
Function and homology information


: / chloroplast thylakoid lumen / chloroplast thylakoid membrane / copper ion binding
Similarity search - Function
Plastocyanin / Blue (type 1) copper protein, plastocyanin-type / Blue (type 1) copper domain / Copper binding proteins, plastocyanin/azurin family / Blue (type 1) copper protein, binding site / Type-1 copper (blue) proteins signature. / Cupredoxins - blue copper proteins / Cupredoxin / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
COPPER (II) ION / Plastocyanin, chloroplastic
Similarity search - Component
Biological speciesSilene latifolia subsp. alba (white campion)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.75 Å
AuthorsSugawara, H. / Inoue, T. / Li, C. / Gotowda, M. / Hibino, T. / Takabe, T. / Kai, Y.
Citation
Journal: J.Biochem.(Tokyo) / Year: 1999
Title: Crystal structures of wild-type and mutant plastocyanins from a higher plant, Silene.
Authors: Sugawara, H. / Inoue, T. / Li, C. / Gotowda, M. / Hibino, T. / Takabe, T. / Kai, Y.
#1: Journal: Acta Crystallogr.,Sect.D / Year: 1997
Title: Crystallization and Preliminary X-Ray Studies of Plastocyanin from Silene Expressed in E. Coli
Authors: Li, C. / Inoue, T. / Gotowda, M. / Hamada, K. / Nishio, N. / Hibino, T. / Takabe, T. / Kai, Y.
#2: Journal: Acta Crystallogr., Sect.B / Year: 1992
Title: Accuracy and Precision in Protein Structure Analysis: Restrained Least-Squares Refinement of the Structure of Poplar Plastocyanin at 1.33 A Resolution
Authors: Guss, J.M. / Bartunik, H.D. / Freeman, H.C.
History
DepositionOct 19, 1998Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 19, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Derived calculations
Category: database_2 / struct_conn ...database_2 / 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 / _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
Revision 1.4Aug 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

Downloads & links

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Assembly

Deposited unit
A: PROTEIN (PLASTOCYANIN)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)10,4792
Polymers10,4161
Non-polymers641
Water1,31573
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)55.900, 55.900, 68.200
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein PROTEIN (PLASTOCYANIN)


Mass: 10415.667 Da / Num. of mol.: 1 / Mutation: E43K, D44K
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Silene latifolia subsp. alba (white campion)
Species: Silene latifolia / Strain: subsp. alba / Organelle: CHLOROPLAST / Production host: Escherichia coli (E. coli) / References: UniProt: P07030
#2: Chemical ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cu
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 73 / 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: 2.54 Å3/Da / Density % sol: 52 %
Crystal growpH: 7
Details: 2.8M AMMONIUM SULFATE, 100MM POTASSIUM PHOSPHATE, pH 7.0
Crystal grow
*PLUS
Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
12.8 Mammonium sulfate1reservoir
2100 mMpotassium phosphate1reservoir
313 mg/mlprotein1drop

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Data collection

DiffractionMean temperature: 300 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418
DetectorType: RIGAKU / Detector: IMAGE PLATE / Date: Jan 15, 1995
RadiationMonochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.75→30 Å / Num. obs: 10737 / % possible obs: 93.6 % / Observed criterion σ(I): 0 / Redundancy: 4.9 % / Rmerge(I) obs: 0.056
Reflection
*PLUS
Num. measured all: 52627

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Processing

Software
NameClassification
AMoREphasing
REFMACrefinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1PCY

1pcy
PDB Unreleased entry


Resolution: 1.75→20 Å / Cross valid method: THROUGHOUT / σ(F): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.199 515 5 %RANDOM
Rwork0.188 ---
obs0.18 10731 93 %-
Refinement stepCycle: LAST / Resolution: 1.75→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms732 0 1 73 806
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONp_bond_d0.0070.005
X-RAY DIFFRACTIONp_angle_d0.0220.01
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d0.0380.05
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it2.522
X-RAY DIFFRACTIONp_mcangle_it3.3373
X-RAY DIFFRACTIONp_scbond_it4.3892
X-RAY DIFFRACTIONp_scangle_it6.1953
X-RAY DIFFRACTIONp_plane_restr
X-RAY DIFFRACTIONp_chiral_restr0.2340.15
X-RAY DIFFRACTIONp_singtor_nbd
X-RAY DIFFRACTIONp_multtor_nbd
X-RAY DIFFRACTIONp_xhyhbond_nbd
X-RAY DIFFRACTIONp_xyhbond_nbd
X-RAY DIFFRACTIONp_planar_tor6.57
X-RAY DIFFRACTIONp_staggered_tor21.315
X-RAY DIFFRACTIONp_orthonormal_tor
X-RAY DIFFRACTIONp_transverse_tor
X-RAY DIFFRACTIONp_special_tor015
Software
*PLUS
Name: REFMAC / Classification: refinement
Refinement
*PLUS
Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor obs: 0.18
Solvent computation
*PLUS
Displacement parameters
*PLUS

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