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- PDB-1kn6: Solution Structure of the Mouse Prohormone Convertase 1 Pro-Domain -

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Basic information

Entry
Database: PDB / ID: 1kn6
TitleSolution Structure of the Mouse Prohormone Convertase 1 Pro-Domain
ComponentsProhormone Convertase 1
KeywordsHYDROLASE / BETA-ALPHA-BETA-BETA-ALPHA-BETA
Function / homology
Function and homology information


proprotein convertase 1 / Peptide hormone biosynthesis / Synthesis, secretion, and deacylation of Ghrelin / insulin processing / response to chlorate / peptide biosynthetic process / pituitary gland development / response to fatty acid / pancreas development / peptide hormone processing ...proprotein convertase 1 / Peptide hormone biosynthesis / Synthesis, secretion, and deacylation of Ghrelin / insulin processing / response to chlorate / peptide biosynthetic process / pituitary gland development / response to fatty acid / pancreas development / peptide hormone processing / protein autoprocessing / response to axon injury / response to glucose / axon terminus / response to glucocorticoid / transport vesicle / response to interleukin-1 / response to nutrient levels / neurogenesis / secretory granule / positive regulation of protein secretion / trans-Golgi network / protein processing / response to peptide hormone / response to calcium ion / perikaryon / secretory granule lumen / endopeptidase activity / response to lipopolysaccharide / response to xenobiotic stimulus / neuron projection / endoplasmic reticulum lumen / serine-type endopeptidase activity / neuronal cell body / dendrite / perinuclear region of cytoplasm / extracellular space / identical protein binding / membrane
Similarity search - Function
Peptidase S8, pro-domain / Prohormone convertase enzyme / Prohormone convertase enzyme / Peptidase S8, pro-domain / Peptidase S8, pro-domain superfamily / Peptidase S8 pro-domain / Kexin/furin catalytic domain / P domain / Proprotein convertase P-domain / P/Homo B domain profile. ...Peptidase S8, pro-domain / Prohormone convertase enzyme / Prohormone convertase enzyme / Peptidase S8, pro-domain / Peptidase S8, pro-domain superfamily / Peptidase S8 pro-domain / Kexin/furin catalytic domain / P domain / Proprotein convertase P-domain / P/Homo B domain profile. / Peptidase S8, subtilisin, His-active site / Serine proteases, subtilase family, histidine active site. / Serine proteases, subtilase family, aspartic acid active site. / Peptidase S8, subtilisin, Asp-active site / Serine proteases, subtilase family, serine active site. / Peptidase S8, subtilisin, Ser-active site / Serine proteases, subtilase domain profile. / Peptidase S8, subtilisin-related / Peptidase S8/S53 domain superfamily / Subtilase family / Peptidase S8/S53 domain / Galactose-binding-like domain superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Neuroendocrine convertase 1
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / simulated annealing
AuthorsTangrea, M.A. / Bryan, P.N. / Sari, N. / Orban, J.
CitationJournal: J.Mol.Biol. / Year: 2002
Title: Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus.
Authors: Tangrea, M.A. / Bryan, P.N. / Sari, N. / Orban, J.
History
DepositionDec 18, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 17, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Dec 21, 2022Group: Database references / Category: struct_ref_seq_dif / Item: _struct_ref_seq_dif.details
Revision 1.5May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Prohormone Convertase 1


Theoretical massNumber of molelcules
Total (without water)10,6711
Polymers10,6711
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 280structures with the lowest energy
RepresentativeModel #3closest to the average

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Components

#1: Protein Prohormone Convertase 1 / Neuroendocrine convertase 1


Mass: 10670.872 Da / Num. of mol.: 1 / Fragment: N-terminal Pro-domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pG5 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P63239, proprotein convertase 1

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1213D 13C-separated NOESY
1313D 15N-separated NOESY
NMR detailsText: This structure was determined using standard 3D heteronuclear techniques

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Sample preparation

Details
Solution-IDContentsSolvent system
1100mM phosphate buffer; uniform (random) labeling with 15N, 13C90% H2O/10% D2O
2100mM phosphate buffer; uniform (random) labeling with 15N, 13C100% D2O
Sample conditionsIonic strength: 2mM / pH: 7.0 / Pressure: ambient / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX6001
Bruker DRXBrukerDRX5002

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Processing

NMR softwareName: NMRPipe / Version: 1.8 / Developer: Delaglio, F., et al / Classification: processing
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 280 / Conformers submitted total number: 20

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