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- PDB-2zg8: Crystal Structure of Pd(allyl)/apo-H49AFr -

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Basic information

Entry
Database: PDB / ID: 2zg8
TitleCrystal Structure of Pd(allyl)/apo-H49AFr
ComponentsFerritin light chain
KeywordsMETAL BINDING PROTEIN / IRON STORAGE PROTEIN / LIGHT CHAIN APOFERRITIN / ARTIFICIAL METALLOPROTEIN
Function / homology
Function and homology information


ferritin complex / autolysosome / ferric iron binding / autophagosome / iron ion transport / ferrous iron binding / cytoplasmic vesicle / intracellular iron ion homeostasis / iron ion binding / cytoplasm
Similarity search - Function
Ferritin iron-binding regions signature 1. / Ferritin iron-binding regions signature 2. / Ferritin, conserved site / Ferritin, core subunit, four-helix bundle / Ferritin / Ferritin / Ferritin-like diiron domain / Ferritin-like diiron domain profile. / Ferritin/DPS protein domain / Ferritin-like domain ...Ferritin iron-binding regions signature 1. / Ferritin iron-binding regions signature 2. / Ferritin, conserved site / Ferritin, core subunit, four-helix bundle / Ferritin / Ferritin / Ferritin-like diiron domain / Ferritin-like diiron domain profile. / Ferritin/DPS protein domain / Ferritin-like domain / Ferritin-like / Ferritin-like superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
: / PALLADIUM ION / Palladium(II) allyl complex / Ferritin light chain
Similarity search - Component
Biological speciesEquus caballus (horse)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsAbe, S. / Niemeyer, J. / Abe, M. / Ueno, T. / Hikage, T. / Erker, G. / Watanabe, Y.
CitationJournal: J.Am.Chem.Soc. / Year: 2008
Title: Control of the coordination structure of organometallic palladium complexes in an apo-ferritin cage.
Authors: Abe, S. / Niemeyer, J. / Abe, M. / Takezawa, Y. / Ueno, T. / Hikage, T. / Erker, G. / Watanabe, Y.
History
DepositionJan 18, 2008Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 26, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 10, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_conn_angle ...database_2 / pdbx_struct_conn_angle / pdbx_struct_special_symmetry / 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_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_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 1.3Nov 1, 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
X: Ferritin light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,26917
Polymers19,7891
Non-polymers1,48016
Water3,801211
1
X: Ferritin light chain
hetero molecules
x 24


Theoretical massNumber of molelcules
Total (without water)510,464408
Polymers474,94424
Non-polymers35,521384
Water43224
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,-y,z1
crystal symmetry operation3_555-x,y,-z1
crystal symmetry operation4_555x,-y,-z1
crystal symmetry operation5_555z,x,y1
crystal symmetry operation6_555z,-x,-y1
crystal symmetry operation7_555-z,-x,y1
crystal symmetry operation8_555-z,x,-y1
crystal symmetry operation9_555y,z,x1
crystal symmetry operation10_555-y,z,-x1
crystal symmetry operation11_555y,-z,-x1
crystal symmetry operation12_555-y,-z,x1
crystal symmetry operation13_555y,x,-z1
crystal symmetry operation14_555-y,-x,-z1
crystal symmetry operation15_555y,-x,z1
crystal symmetry operation16_555-y,x,z1
crystal symmetry operation17_555x,z,-y1
crystal symmetry operation18_555-x,z,y1
crystal symmetry operation19_555-x,-z,-y1
crystal symmetry operation20_555x,-z,y1
crystal symmetry operation21_555z,y,-x1
crystal symmetry operation22_555z,-y,x1
crystal symmetry operation23_555-z,y,x1
crystal symmetry operation24_555-z,-y,-x1
Buried area110470 Å2
ΔGint-1375 kcal/mol
Surface area137730 Å2
MethodPISA
Unit cell
Length a, b, c (Å)181.339, 181.339, 181.339
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number209
Space group name H-MF432
Components on special symmetry positions
IDModelComponents
11X-176-

CD

21X-233-

HOH

31X-244-

HOH

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Components

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Protein , 1 types, 1 molecules X

#1: Protein Ferritin light chain / Ferritin L subunit


Mass: 19789.314 Da / Num. of mol.: 1 / Mutation: H49A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Equus caballus (horse) / Gene: FTL / Plasmid: pMK2 / Production host: Escherichia coli (E. coli) / Strain (production host): Nova Blue / References: UniProt: P02791

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Non-polymers , 6 types, 227 molecules

#2: Chemical ChemComp-PD / PALLADIUM ION


Mass: 106.420 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Pd
#3: Chemical ChemComp-CD / CADMIUM ION


Mass: 112.411 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cd
#4: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-PLL / Palladium(II) allyl complex


Mass: 147.492 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H5Pd
#6: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C2H6O2
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 211 / Source method: isolated from a natural source / Formula: H2O

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Details

Nonpolymer detailsIN THE LIGAND PLL, ALL C-C BOND TYPES ARE DELOCALIZED BONDS AND PD-C BONDS ARE PI BONDS.
Sequence detailsTHE FEATURE OF UNIPROT (FRIL_HORSE, P02791) SHOWS CONFLICT AT THIS POSITION: L -> P (IN REF. 2).

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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: 3.14 Å3/Da / Density % sol: 60.81 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: ammonium sulfate, cadmium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å
DetectorType: RIGAKU RAXIS VII / Detector: IMAGE PLATE / Date: Aug 20, 2007
RadiationMonochromator: CONFOCAL MIRROS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.6→50 Å / Num. obs: 34183 / % possible obs: 100 % / Redundancy: 17.8 % / Biso Wilson estimate: 18.007 Å2 / Rmerge(I) obs: 0.062
Reflection shellResolution: 1.6→1.66 Å / Redundancy: 8.7 % / Rmerge(I) obs: 0.284 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1DAT

1dat


Resolution: 1.6→25.15 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.945 / SU B: 1.168 / SU ML: 0.042 / Cross valid method: THROUGHOUT / ESU R: 0.079 / ESU R Free: 0.079 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.2111 1728 5.1 %RANDOM
Rwork0.18751 ---
obs0.18869 32427 99.94 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 18.223 Å2
Refinement stepCycle: LAST / Resolution: 1.6→25.15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1451 0 62 211 1724
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0221538
X-RAY DIFFRACTIONr_angle_refined_deg1.0982.0252081
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.4295196
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.27524.07481
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.25515279
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.3021514
X-RAY DIFFRACTIONr_chiral_restr0.0840.2225
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.021150
X-RAY DIFFRACTIONr_nbd_refined0.2080.2814
X-RAY DIFFRACTIONr_nbtor_refined0.3050.21061
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1180.2163
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1860.281
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1460.236
X-RAY DIFFRACTIONr_mcbond_it0.6871.5907
X-RAY DIFFRACTIONr_mcangle_it1.18121432
X-RAY DIFFRACTIONr_scbond_it2.083678
X-RAY DIFFRACTIONr_scangle_it3.3984.5616
X-RAY DIFFRACTIONr_sphericity_free16.52432
X-RAY DIFFRACTIONr_sphericity_bonded7.83333
LS refinement shellResolution: 1.601→1.642 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.309 110 -
Rwork0.255 2353 -
obs--100 %

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