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- PDB-6eqv: X-ray structure of the proprotein convertase furin bound with the... -

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Basic information

Entry
Database: PDB / ID: 6eqv
TitleX-ray structure of the proprotein convertase furin bound with the competitive inhibitor Phac-Cit-Val-Arg-Amba
Components
  • Furin
  • HY1-LLI-VAL-ARG-00S
KeywordsHYDROLASE / Protease / Inhibitor / Complex / Proprotein convertase / Citrullin
Function / homology
Function and homology information


Signaling by PDGF / Amyloid fiber formation / Assembly of active LPL and LIPC lipase complexes / Formation of the cornified envelope / Uptake and function of anthrax toxins / TGF-beta receptor signaling activates SMADs / Signaling by NODAL / Pre-NOTCH Processing in Golgi / Synthesis and processing of ENV and VPU / NGF processing ...Signaling by PDGF / Amyloid fiber formation / Assembly of active LPL and LIPC lipase complexes / Formation of the cornified envelope / Uptake and function of anthrax toxins / TGF-beta receptor signaling activates SMADs / Signaling by NODAL / Pre-NOTCH Processing in Golgi / Synthesis and processing of ENV and VPU / NGF processing / Removal of aminoterminal propeptides from gamma-carboxylated proteins / Activation of Matrix Metalloproteinases / Elastic fibre formation / Collagen degradation / zymogen inhibition / positive regulation of transforming growth factor beta1 activation / dibasic protein processing / furin / nerve growth factor production / regulation of lipoprotein lipase activity / nerve growth factor processing / regulation of low-density lipoprotein particle receptor biosynthetic process / negative regulation of low-density lipoprotein particle receptor catabolic process / signal peptide processing / negative regulation of transforming growth factor beta1 production / peptide biosynthetic process / peptide hormone processing / secretion by cell / integral component of Golgi membrane / nerve growth factor binding / cornification / trans-Golgi network transport vesicle / regulation of endopeptidase activity / zymogen activation / positive regulation of membrane protein ectodomain proteolysis / regulation of protein catabolic process / regulation of signal transduction / protein processing / collagen catabolic process / extracellular matrix disassembly / peptide binding / viral protein processing / trans-Golgi network / viral life cycle / serine-type endopeptidase inhibitor activity / transforming growth factor beta receptor signaling pathway / Golgi lumen / extracellular matrix organization / peptidase activity / endopeptidase activity / endosome membrane / protease binding / membrane raft / Golgi membrane / serine-type endopeptidase activity / cellular protein metabolic process / endoplasmic reticulum / cell surface / extracellular exosome / membrane / extracellular region / plasma membrane / metal ion binding
Growth factor receptor cysteine-rich domain superfamily / Peptidase S8, pro-domain / Peptidase S8, subtilisin, Ser-active site / Peptidase S8/S53 domain superfamily / Peptidase S8, pro-domain superfamily / Peptidase S8, subtilisin, Asp-active site / Peptidase S8, subtilisin, His-active site / Peptidase S8, subtilisin-related / Subtilase family / Proprotein convertase P-domain ...Growth factor receptor cysteine-rich domain superfamily / Peptidase S8, pro-domain / Peptidase S8, subtilisin, Ser-active site / Peptidase S8/S53 domain superfamily / Peptidase S8, pro-domain superfamily / Peptidase S8, subtilisin, Asp-active site / Peptidase S8, subtilisin, His-active site / Peptidase S8, subtilisin-related / Subtilase family / Proprotein convertase P-domain / Peptidase S8/S53 domain / P domain / Peptidase S8 pro-domain / Serine proteases, subtilase family, aspartic acid active site. / Serine proteases, subtilase family, histidine active site. / Furin-like repeat / Serine proteases, subtilase family, serine active site. / P/Homo B domain profile. / Galactose-binding-like domain superfamily / Kexin/furin catalytic domain
Furin
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.895 Å
AuthorsDahms, S.O. / Than, M.E.
CitationJournal: Biochemistry / Year: 2018
Title: X-ray Structures of the Proprotein Convertase Furin Bound with Substrate Analogue Inhibitors Reveal Substrate Specificity Determinants beyond the S4 Pocket.
Authors: Dahms, S.O. / Hardes, K. / Steinmetzer, T. / Than, M.E.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Oct 16, 2017 / Release: Feb 28, 2018
RevisionDateData content typeProviderType
1.0Feb 28, 2018Structure modelrepositoryInitial release

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: Furin
D: HY1-LLI-VAL-ARG-00S
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,30110
Polymers53,0532
Non-polymers2488
Water9,188510
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2240 Å2
ΔGint-53 kcal/mol
Surface area17580 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)131.601, 131.601, 155.638
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number179
Space group name H-MP6522
Components on special symmetry positions
IDModelComponents
11A-606-

NA

21A-607-

NA

31A-1139-

HOH

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Components

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Protein/peptide , 2 types, 2 molecules AD

#1: Protein/peptide Furin / / Dibasic-processing enzyme / Paired basic amino acid residue-cleaving enzyme / PACE


Mass: 52388.602 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FURIN, FUR, PACE, PCSK3 / Cell line (production host): HEK293S / Production host: Homo sapiens (human) / References: UniProt: P09958, furin
#2: Protein/peptide HY1-LLI-VAL-ARG-00S


Mass: 664.822 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 4 types, 518 molecules

#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca / Calcium
#4: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Na / Sodium
#5: Chemical ChemComp-CL / CHLORIDE ION


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


Mass: 18.015 Da / Num. of mol.: 510 / Source method: isolated from a natural source / Formula: H2O / Water

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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: 3.67 Å3/Da / Density % sol: 66.45 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop
Details: CRYSTALLIZATION SOLUTION: 100mM MES, 200mM K/NaH2PO4, PH 5.5-6.0, 3-4M NaCl, 3% DMSO; RESERVOIR SOLUTION: 3-4 M NaCl

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.918409 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 24, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.918409 Å / Relative weight: 1
ReflectionResolution: 1.89→47.2 Å / Num. obs: 63141 / % possible obs: 99.4 % / Redundancy: 6.54 % / Biso Wilson estimate: 20.9 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.109 / Rrim(I) all: 0.118 / Net I/σ(I): 14.97
Reflection shellResolution: 1.89→2.01 Å / Rmerge(I) obs: 0.723 / Mean I/σ(I) obs: 2.84 / Num. unique obs: 9981 / CC1/2: 0.844 / Rrim(I) all: 0.786

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
XDSdata reduction
XDSdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5JXH
Resolution: 1.895→45.976 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 17.64
RfactorNum. reflection% reflection
Rfree0.1821 3065 4.85 %
Rwork0.1637 --
Obs0.1646 63131 99.44 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.895→45.976 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3657 0 8 510 4175
Refine LS restraints

Refinement-ID: X-RAY DIFFRACTION

TypeDev idealNumber
f_bond_d0.0063786
f_angle_d0.835166
f_dihedral_angle_d22.062256
f_chiral_restr0.054560
f_plane_restr0.005688
LS refinement shell

Refinement-ID: X-RAY DIFFRACTION

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.8949-1.92460.29991420.2443262797
1.9246-1.95610.25571270.2253271199
1.9561-1.98980.2821210.2113268599
1.9898-2.0260.2181360.2097268099
2.026-2.0650.221340.19152689100
2.065-2.10710.21881530.1798267799
2.1071-2.1530.18371380.17322699100
2.153-2.2030.22881390.1718267899
2.203-2.25810.19191330.169270199
2.2581-2.31920.21731260.1699271099
2.3192-2.38740.17691250.16272715100
2.3874-2.46450.17471280.1732711100
2.4645-2.55260.19161360.16882729100
2.5526-2.65470.19931240.17272742100
2.6547-2.77560.19021520.17282717100
2.7756-2.92190.21781480.17682743100
2.9219-3.10490.15721400.17352738100
3.1049-3.34460.19281510.15382766100
3.3446-3.6810.15531540.14142760100
3.681-4.21330.14561460.12532791100
4.2133-5.30710.1361520.12872831100
5.3071-45.98960.16561600.1753296699

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