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- PDB-9h7p: Human Transthyretin S52P Mutant in Complex with 4-(1H-pyrazol-4-y... -

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Basic information

Entry
Database: PDB / ID: 9h7p
TitleHuman Transthyretin S52P Mutant in Complex with 4-(1H-pyrazol-4-yl)quinoline
ComponentsTransthyretin
KeywordsTRANSPORT PROTEIN / Amyloidosis / Retinol / Thyroxine / RBP
Function / homology
Function and homology information


Defective visual phototransduction due to STRA6 loss of function / negative regulation of glomerular filtration / The canonical retinoid cycle in rods (twilight vision) / hormone binding / purine nucleobase metabolic process / Non-integrin membrane-ECM interactions / molecular sequestering activity / phototransduction, visible light / retinoid metabolic process / Retinoid metabolism and transport ...Defective visual phototransduction due to STRA6 loss of function / negative regulation of glomerular filtration / The canonical retinoid cycle in rods (twilight vision) / hormone binding / purine nucleobase metabolic process / Non-integrin membrane-ECM interactions / molecular sequestering activity / phototransduction, visible light / retinoid metabolic process / Retinoid metabolism and transport / hormone activity / azurophil granule lumen / Amyloid fiber formation / Neutrophil degranulation / protein-containing complex binding / protein-containing complex / extracellular space / extracellular exosome / extracellular region / identical protein binding
Similarity search - Function
Transthyretin, conserved site / Transthyretin signature 2. / Transthyretin, thyroxine binding site / Transthyretin signature 1. / Transthyretin / Transthyretin/hydroxyisourate hydrolase / Transthyretin/hydroxyisourate hydrolase domain / Transthyretin/hydroxyisourate hydrolase domain superfamily / HIUase/Transthyretin family
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.36 Å
AuthorsChen, W.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
University of College LondonBXTX United Kingdom
Other privateHN9A
Citation
Journal: Plos One / Year: 2025
Title: Fragment-based drug discovery for transthyretin kinetic stabilisers using a novel capillary zone electrophoresis method.
Authors: Chen, W.
#1: Journal: Biorxiv / Year: 2025
Title: Fragment-Based Drug Discovery for Transthyretin Kinetic Stabilisers Using a Novel Capillary Zone Electrophoresis Method
Authors: Chen, W.
History
DepositionOct 27, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 12, 2025Provider: repository / Type: Initial release
Revision 1.1May 28, 2025Group: Database references / Category: citation / citation_author

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Transthyretin
B: Transthyretin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,0456
Polymers27,5752
Non-polymers4714
Water1,76598
1
A: Transthyretin
B: Transthyretin
hetero molecules

A: Transthyretin
B: Transthyretin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,09112
Polymers55,1504
Non-polymers9418
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_545-x,-y-1,z1
Unit cell
Length a, b, c (Å)84.864, 41.902, 63.589
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11A-202-

A1ISS

21A-202-

A1ISS

31A-202-

A1ISS

41B-202-

A1ISS

51B-202-

A1ISS

61B-202-

A1ISS

71B-202-

A1ISS

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Components

#1: Protein Transthyretin / ATTR / Prealbumin / TBPA


Mass: 13787.397 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Tissue: Blood / Gene: TTR, PALB / Production host: Escherichia coli (E. coli) / References: UniProt: P02766
#2: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#3: Chemical ChemComp-A1ISS / 4-(1H-pyrazol-4-yl)quinoline


Mass: 195.220 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C12H9N3 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 98 / Source method: isolated from a natural source / Formula: H2O
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: 2.05 Å3/Da / Density % sol: 40 %
Crystal growTemperature: 294.15 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: 100 mM HEPES, 200 mM CaCl2, 28% v/v PEG400, pH 7.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: May 29, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 1.36→41.9 Å / Num. obs: 49469 / % possible obs: 99.6 % / Redundancy: 4.6 % / Rmerge(I) obs: 0.055 / Rpim(I) all: 0.031 / Net I/σ(I): 10.9
Reflection shellResolution: 1.36→1.39 Å / Rmerge(I) obs: 0.525 / Mean I/σ(I) obs: 2.1 / Num. unique obs: 3607 / Rpim(I) all: 0.306

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Processing

Software
NameVersionClassification
REFMAC5.7.0032refinement
xia2data reduction
xia2data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.36→35.3 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.956 / SU B: 2.069 / SU ML: 0.038 / Cross valid method: THROUGHOUT / ESU R: 0.057 / ESU R Free: 0.057 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20509 2503 5.1 %RANDOM
Rwork0.16517 ---
obs0.16717 46910 99.37 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 17.157 Å2
Baniso -1Baniso -2Baniso -3
1--0.05 Å2-0 Å20 Å2
2--0.03 Å20 Å2
3---0.01 Å2
Refinement stepCycle: 1 / Resolution: 1.36→35.3 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1705 0 32 98 1835
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0220.0191819
X-RAY DIFFRACTIONr_bond_other_d0.0020.021638
X-RAY DIFFRACTIONr_angle_refined_deg2.1111.9622496
X-RAY DIFFRACTIONr_angle_other_deg0.97233771
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.415235
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.26423.38565
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.0415252
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.56155
X-RAY DIFFRACTIONr_chiral_restr0.1310.2284
X-RAY DIFFRACTIONr_gen_planes_refined0.0140.0212045
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02412
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.6771.539919
X-RAY DIFFRACTIONr_mcbond_other2.6761.54920
X-RAY DIFFRACTIONr_mcangle_it3.3352.3091146
X-RAY DIFFRACTIONr_mcangle_other3.3352.3121147
X-RAY DIFFRACTIONr_scbond_it3.9911.862900
X-RAY DIFFRACTIONr_scbond_other3.9891.862901
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.5132.671346
X-RAY DIFFRACTIONr_long_range_B_refined4.35113.9342040
X-RAY DIFFRACTIONr_long_range_B_other4.3513.9362041
X-RAY DIFFRACTIONr_rigid_bond_restr6.22733457
X-RAY DIFFRACTIONr_sphericity_free15.717527
X-RAY DIFFRACTIONr_sphericity_bonded10.67153473
LS refinement shellResolution: 1.36→1.393 Å
RfactorNum. reflection% reflection
Rfree0.332 171 -
Rwork0.282 3425 -
obs--99.39 %

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