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- PDB-1bht: NK1 FRAGMENT OF HUMAN HEPATOCYTE GROWTH FACTOR -

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Basic information

Entry
Database: PDB / ID: 1bht
TitleNK1 FRAGMENT OF HUMAN HEPATOCYTE GROWTH FACTOR
ComponentsHEPATOCYTE GROWTH FACTOR
KeywordsHEPARIN-BINDING DOMAIN / KRINGLE / C-MET RECEPTOR ANGONIST/ ANTAGONIST / GROWTH FACTOR
Function / homology
Function and homology information


regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling / Drug-mediated inhibition of MET activation / MET activates STAT3 / negative regulation of hydrogen peroxide-mediated programmed cell death / MET Receptor Activation / MET interacts with TNS proteins / MET receptor recycling / cellular response to hepatocyte growth factor stimulus / MET activates PTPN11 / hepatocyte growth factor receptor signaling pathway ...regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling / Drug-mediated inhibition of MET activation / MET activates STAT3 / negative regulation of hydrogen peroxide-mediated programmed cell death / MET Receptor Activation / MET interacts with TNS proteins / MET receptor recycling / cellular response to hepatocyte growth factor stimulus / MET activates PTPN11 / hepatocyte growth factor receptor signaling pathway / MET activates RAP1 and RAC1 / MET activates PI3K/AKT signaling / MET activates PTK2 signaling / positive regulation of DNA biosynthetic process / negative regulation of release of cytochrome c from mitochondria / chemoattractant activity / positive regulation of osteoblast differentiation / epithelial to mesenchymal transition / MET activates RAS signaling / platelet alpha granule lumen / negative regulation of autophagy / Interleukin-7 signaling / growth factor activity / cell chemotaxis / Negative regulation of MET activity / Constitutive Signaling by Aberrant PI3K in Cancer / Platelet degranulation / mitotic cell cycle / PIP3 activates AKT signaling / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / Interleukin-4 and Interleukin-13 signaling / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of MAPK cascade / positive regulation of cell migration / signaling receptor binding / negative regulation of apoptotic process / positive regulation of transcription by RNA polymerase II / extracellular region / membrane / identical protein binding
Similarity search - Function
Hepatocyte growth factor / Hepatocyte growth factor/Macrophage stimulatory protein / Hepatocyte Growth Factor / Hepatocyte Growth Factor / Plasminogen Kringle 4 / Plasminogen Kringle 4 / divergent subfamily of APPLE domains / : / PAN/Apple domain profile. / PAN domain ...Hepatocyte growth factor / Hepatocyte growth factor/Macrophage stimulatory protein / Hepatocyte Growth Factor / Hepatocyte Growth Factor / Plasminogen Kringle 4 / Plasminogen Kringle 4 / divergent subfamily of APPLE domains / : / PAN/Apple domain profile. / PAN domain / PAN/Apple domain / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / Kringle-like fold / 3-Layer(bba) Sandwich / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan / Beta Barrel / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Hepatocyte growth factor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2 Å
AuthorsUltsch, M.H. / Lokker, N.A. / Godowski, P.J. / De Vos, A.M.
CitationJournal: Structure / Year: 1998
Title: Crystal structure of the NK1 fragment of human hepatocyte growth factor at 2.0 A resolution.
Authors: Ultsch, M. / Lokker, N.A. / Godowski, P.J. / de Vos, A.M.
History
DepositionJun 10, 1998Processing site: BNL
Revision 1.0Nov 4, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 16, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HEPATOCYTE GROWTH FACTOR
B: HEPATOCYTE GROWTH FACTOR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,3837
Polymers40,6192
Non-polymers7655
Water4,792266
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3000 Å2
ΔGint-46 kcal/mol
Surface area18150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)88.320, 88.320, 117.284
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(-0.808389, 0.57115, 0.142463), (0.584002, 0.747812, 0.315785), (0.073825, 0.338476, -0.938075)100.2944, -52.5168, 99.6606
2given(-0.784321, 0.602051, 0.14958), (0.603961, 0.686, 0.405753), (0.141672, 0.408581, -0.90166)97.2267, -56.5677, 91.3531

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Components

#1: Protein HEPATOCYTE GROWTH FACTOR / NK1


Mass: 20309.295 Da / Num. of mol.: 2
Fragment: NK1 FRAGMENT, HEPARIN BINDING DOMAIN PLUS C-MET BINDING DOMAIN
Source method: isolated from a genetically manipulated source
Details: HEPES BUFFER MOLECULE BOUND IN KRINGLE BINDING POCKET
Source: (gene. exp.) Homo sapiens (human) / Cellular location: CYTOPLASM / Plasmid: PF-NK1 / Production host: Escherichia coli (E. coli) / Strain (production host): 27C7 / References: UniProt: P14210
#2: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#3: Chemical ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES


Mass: 238.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H18N2O4S / Comment: pH buffer*YM
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 266 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 7

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Sample preparation

CrystalDensity Matthews: 2.82 Å3/Da / Density % sol: 56 %
Crystal growpH: 7.5
Details: 40% PEG 3400, 0.1M HEPES PH 7.5, 0.3M AMMONIUM SULFATE. PROTEIN CONCENTRATION OF 3MG/ML
Crystal
*PLUS
Crystal grow
*PLUS
Method: vapor diffusion, sitting drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
13 mg/mlprotein1drop
220 %PEG34001reservoir
30.1 MHEPES1reservoir
40.3 Mammonium sulfate1reservoir

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Data collection

DiffractionMean temperature: 287 K
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.908
DetectorType: FUJI / Detector: IMAGE PLATE / Date: Jan 1, 1994 / Details: COLLIMATOR
RadiationMonochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.908 Å / Relative weight: 1
ReflectionHighest resolution: 2 Å / Num. obs: 1807 / % possible obs: 94 % / Observed criterion σ(I): 0 / Redundancy: 5.2 % / Rmerge(I) obs: 0.066 / Rsym value: 0.056 / Net I/σ(I): 11.7
Reflection shellResolution: 2→2.09 Å / Redundancy: 3 % / Rmerge(I) obs: 0.17 / Rsym value: 0.26 / % possible all: 87

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
RefinementMethod to determine structure: MIR / Resolution: 2→10 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.247 1807 6 %RANDOM
Rwork0.196 ---
obs0.196 29855 94 %-
Displacement parametersBiso mean: 37.4 Å2
Refinement stepCycle: LAST / Resolution: 2→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2822 0 45 266 3133
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.013
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg2.051
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it1.9
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it2.8
X-RAY DIFFRACTIONx_scangle_it
Refine LS restraints NCSNCS model details: NONRESTRAINED
LS refinement shellResolution: 2→2.09 Å / Total num. of bins used: 8
RfactorNum. reflection% reflection
Rfree0.313 183 5 %
Rwork0.292 3105 -
obs--84 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARAM19X.PROTOPHCSDX.PRO
X-RAY DIFFRACTION2PARAM19.SOLTOPH19.SOL
X-RAY DIFFRACTION3HEPS.PARMHEPS.TOP
X-RAY DIFFRACTION4SO4.PARMSO4.TOP

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