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- PDB-9kn8: Crystal structure of Horse spleen L-ferritin mutant (E53F/E56F/E5... -

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Basic information

Entry
Database: PDB / ID: 9kn8
TitleCrystal structure of Horse spleen L-ferritin mutant (E53F/E56F/E57F/R59F/E60F/E63F) with Coumarin 153
ComponentsFerritin light chain
KeywordsMETAL BINDING PROTEIN / 24mer cage / Phenyl Alanine mutant / Coumarin 153
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 / Ferritin-like diiron domain / Ferritin-like diiron domain profile. / Ferritin/DPS protein domain / Ferritin-like domain / Ferritin-like / Ferritin-like superfamily
Similarity search - Domain/homology
: / : / Ferritin light chain
Similarity search - Component
Biological speciesEquus caballus (horse)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.64 Å
AuthorsSuzuki, T. / Hishikawa, Y. / Maity, B. / Abe, S. / Ueno, T.
Funding support Japan, 1items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS) Japan
CitationJournal: Adv Sci / Year: 2025
Title: Design of Aromatic Interaction Networks in a Protein Cage Modulated by Fluorescent Ligand Binding.
Authors: Hishikawa, Y. / Suzuki, T. / Maity, B. / Noya, H. / Yoshizawa, M. / Asanuma, A. / Katagiri, Y. / Abe, S. / Nagatoishi, S. / Tsumoto, K. / Ueno, T.
History
DepositionNov 18, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 5, 2025Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2025Group: Database references / Category: citation / Item: _citation.journal_volume

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ferritin light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,14212
Polymers19,9531
Non-polymers1,18911
Water3,549197
1
A: Ferritin light chain
hetero molecules
x 24


Theoretical massNumber of molelcules
Total (without water)507,402288
Polymers478,86524
Non-polymers28,537264
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 area119350 Å2
ΔGint-378 kcal/mol
Surface area135350 Å2
MethodPISA
Unit cell
Length a, b, c (Å)181.158, 181.158, 181.158
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
11A-202-

CD

21A-203-

CD

31A-204-

CD

41A-207-

A1L54

51A-207-

A1L54

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Ferritin light chain / Ferritin L subunit


Mass: 19952.709 Da / Num. of mol.: 1 / Mutation: E53F/E56F/E57F/R59F/E60F/E63F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Equus caballus (horse) / Gene: FTL / Production host: Escherichia coli (E. coli) / References: UniProt: P02791

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Non-polymers , 6 types, 208 molecules

#2: Chemical
ChemComp-CD / CADMIUM ION


Mass: 112.411 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cd
#3: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#4: Chemical ChemComp-A1L54 / Coumarin 153 / 6-(trifluoromethyl)-3-oxa-13-azatetracyclo[7.7.1.0^{2,7}.0^{13,17}]heptadeca-1(17),2(7),5,8-tetraen-4-one


Mass: 309.283 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H14F3NO2 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 197 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationN

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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: 3.1 Å3/Da / Density % sol: 60.37 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: Ammonium sulfate, Cadmium sulfate / Temp details: Incubation

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Data collection

DiffractionMean temperature: 93 K / Ambient temp details: Liquid N2 vapour / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU FR-E DW / Wavelength: 1.54184 Å
DetectorType: RIGAKU HyPix-6000HE / Detector: PIXEL / Date: Mar 8, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54184 Å / Relative weight: 1
ReflectionResolution: 1.64→18.21 Å / Num. obs: 31536 / % possible obs: 99.5 % / Redundancy: 8.4 % / CC1/2: 0.999 / Rmerge(I) obs: 0.071 / Rpim(I) all: 0.024 / Rrim(I) all: 0.075 / Χ2: 0.98 / Net I/σ(I): 20.9
Reflection shellResolution: 1.64→1.67 Å / Redundancy: 5.2 % / Rmerge(I) obs: 0.815 / Mean I/σ(I) obs: 2.1 / Num. unique obs: 1587 / CC1/2: 0.819 / Rpim(I) all: 0.378 / Rrim(I) all: 0.903 / Χ2: 1.15 / % possible all: 99.4

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Processing

Software
NameVersionClassification
CrysalisProdata collection
CrysalisProdata reduction
Aimlessdata scaling
MOLREPphasing
REFMAC5refinement
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1DAT

1dat


Resolution: 1.64→18.21 Å / SU ML: 0.14 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 21.77 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2082 1588 5.06 %
Rwork0.1925 --
obs0.1933 31414 99.06 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.64→18.21 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1391 0 45 197 1633
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0151527
X-RAY DIFFRACTIONf_angle_d1.7292073
X-RAY DIFFRACTIONf_dihedral_angle_d14.468583
X-RAY DIFFRACTIONf_chiral_restr0.099222
X-RAY DIFFRACTIONf_plane_restr0.011267
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.64-1.690.29011350.24722668X-RAY DIFFRACTION99
1.69-1.750.28051450.23872656X-RAY DIFFRACTION100
1.75-1.820.24571590.23612631X-RAY DIFFRACTION99
1.82-1.910.23891270.22742659X-RAY DIFFRACTION98
1.91-2.010.22731480.21092647X-RAY DIFFRACTION99
2.01-2.130.20691410.1892702X-RAY DIFFRACTION99
2.13-2.30.16841360.18282688X-RAY DIFFRACTION99
2.3-2.530.22111560.18542716X-RAY DIFFRACTION99
2.53-2.890.21571450.18252708X-RAY DIFFRACTION99
2.89-3.640.19331480.17412789X-RAY DIFFRACTION99
3.64-18.210.17981480.17982962X-RAY DIFFRACTION99

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