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- PDB-1bmp: BONE MORPHOGENETIC PROTEIN-7 -

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Basic information

Entry
Database: PDB / ID: 1bmp
TitleBONE MORPHOGENETIC PROTEIN-7
ComponentsBONE MORPHOGENETIC PROTEIN-7
KeywordsTRANSFORMING GROWTH FACTOR / MORPHOGEN / CYTOKINE / BONE / CARTILAGE / GLYCOPROTEIN
Function / homology
Function and homology information


negative regulation of glomerular mesangial cell proliferation / positive regulation of cardiac neural crest cell migration involved in outflow tract morphogenesis / neural fold elevation formation / positive regulation of hyaluranon cable assembly / chorio-allantoic fusion / metanephric mesenchyme morphogenesis / nephrogenic mesenchyme morphogenesis / negative regulation of striated muscle cell apoptotic process / metanephric mesenchymal cell proliferation involved in metanephros development / pericardium morphogenesis ...negative regulation of glomerular mesangial cell proliferation / positive regulation of cardiac neural crest cell migration involved in outflow tract morphogenesis / neural fold elevation formation / positive regulation of hyaluranon cable assembly / chorio-allantoic fusion / metanephric mesenchyme morphogenesis / nephrogenic mesenchyme morphogenesis / negative regulation of striated muscle cell apoptotic process / metanephric mesenchymal cell proliferation involved in metanephros development / pericardium morphogenesis / cardiac septum morphogenesis / mesenchyme development / allantois development / pharyngeal system development / mesonephros development / monocyte aggregation / regulation of removal of superoxide radicals / hindbrain development / metanephros development / heart trabecula morphogenesis / mesenchymal cell differentiation / eye development / negative regulation of mitotic nuclear division / BMP receptor binding / endocardial cushion formation / cellular response to BMP stimulus / ureteric bud development / response to vitamin D / cartilage development / positive regulation of dendrite development / negative regulation of non-canonical NF-kappaB signal transduction / positive regulation of heterotypic cell-cell adhesion / cardiac muscle tissue development / negative regulation of neuron differentiation / Molecules associated with elastic fibres / negative regulation of cell cycle / positive regulation of bone mineralization / dendrite development / positive regulation of osteoblast differentiation / positive regulation of SMAD protein signal transduction / BMP signaling pathway / epithelial to mesenchymal transition / skeletal system development / positive regulation of brown fat cell differentiation / positive regulation of epithelial to mesenchymal transition / Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 / neuron projection morphogenesis / cytokine activity / growth factor activity / response to peptide hormone / osteoblast differentiation / heart development / response to estradiol / heparin binding / cellular response to hypoxia / extracellular matrix / vesicle / negative regulation of DNA-templated transcription / positive regulation of gene expression / positive regulation of DNA-templated transcription / : / extracellular region
Similarity search - Function
TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family / Cystine Knot Cytokines, subunit B / Cystine-knot cytokines / Transforming growth factor-beta, C-terminal / Transforming growth factor beta like domain ...TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family / Cystine Knot Cytokines, subunit B / Cystine-knot cytokines / Transforming growth factor-beta, C-terminal / Transforming growth factor beta like domain / TGF-beta family profile. / Cystine-knot cytokine / Ribbon / Mainly Beta
Similarity search - Domain/homology
Bone morphogenetic protein 7
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / Resolution: 2.8 Å
AuthorsGriffith, D.L. / Scott, D.L.
Citation
Journal: Proc.Natl.Acad.Sci.USA / Year: 1996
Title: Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily.
Authors: Griffith, D.L. / Keck, P.C. / Sampath, T.K. / Rueger, D.C. / Carlson, W.D.
#1: Journal: J.Mol.Biol. / Year: 1994
Title: Crystallization and Preliminary Crystallographic Data of Recombinant Human Osteogenic Protein-1 (Hop-1)
Authors: Griffith, D.L. / Oppermann, H. / Rueger, D.C. / Sampath, T.K. / Tucker, R.F. / Carlson, W.D.
History
DepositionDec 14, 1995Processing site: BNL
Revision 1.0Jul 23, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Jun 5, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: BONE MORPHOGENETIC PROTEIN-7


Theoretical massNumber of molelcules
Total (without water)15,7001
Polymers15,7001
Non-polymers00
Water00
1
A: BONE MORPHOGENETIC PROTEIN-7

A: BONE MORPHOGENETIC PROTEIN-7


Theoretical massNumber of molelcules
Total (without water)31,3992
Polymers31,3992
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_555y,x,-z1
Buried area2370 Å2
ΔGint-26 kcal/mol
Surface area11690 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)99.460, 99.460, 42.090
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

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Components

#1: Protein BONE MORPHOGENETIC PROTEIN-7 / OSTEOGENIC PROTEIN-1 / HOP-1 / BMP-7


Mass: 15699.730 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Description: REFERENCE, T.K. SAMPATH, ET AL. (1992) J. BIOL. CHEM. 267, 20452-20362
Gene: HOP-1 CDNA / Organ: OVARY / Gene (production host): HOP-1 CDNA / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P18075
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.83 Å3/Da / Density % sol: 60 %
Crystal
*PLUS
Density % sol: 62 %
Crystal grow
*PLUS
Temperature: 22 ℃ / pH: 5 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
15 mg/mlprotein1drop
24 %satammonium sulfate1drop
325 mMsodium acetate1drop
48 %satammonium sulfate1reservoir
550 mMsodium acetate1reservoir

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Data collection

Diffraction sourceWavelength: 1.5418
DetectorType: RIGAKU / Detector: IMAGE PLATE / Date: Nov 30, 1993
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionNum. obs: 5502 / % possible obs: 87 % / Observed criterion σ(I): 2 / Redundancy: 2.6 % / Rmerge(I) obs: 0.067
Reflection
*PLUS
Highest resolution: 2.8 Å

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Processing

Software
NameVersionClassification
R-AXISSOFTWAREdata collection
R-AXISSOFTWAREdata reduction
X-PLORmodel building
PROFFTrefinement
X-PLORrefinement
R-AXISdata scaling
X-PLORphasing
RefinementResolution: 2.8→10 Å / σ(F): 2
Details: LOOP REGION (RESIDUES 118 - 122) IS DISORDERED AND MODELED STEREOCHEMICALLY. NOTE THAT RESIDUE 59 IS DESCRIBED AS TRANS IN THE PAPER CITED ON JRNL RECORDS ABOVE BUT THE CURRENT MODEL ...Details: LOOP REGION (RESIDUES 118 - 122) IS DISORDERED AND MODELED STEREOCHEMICALLY. NOTE THAT RESIDUE 59 IS DESCRIBED AS TRANS IN THE PAPER CITED ON JRNL RECORDS ABOVE BUT THE CURRENT MODEL PRESENTED IN THIS ENTRY HAS RESIDUE 59 AS CIS.
RfactorNum. reflection
Rfree0.308 -
Rwork0.227 -
obs-5418
Displacement parametersBiso mean: 28.48 Å2
Refine analyzeLuzzati coordinate error obs: 0.25 Å
Refinement stepCycle: LAST / Resolution: 2.8→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms828 0 0 0 828
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONp_bond_d0.0080.03
X-RAY DIFFRACTIONp_angle_d0.0250.05
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d0.1380.1
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it
X-RAY DIFFRACTIONp_mcangle_it
X-RAY DIFFRACTIONp_scbond_it
X-RAY DIFFRACTIONp_scangle_it
X-RAY DIFFRACTIONp_plane_restr0.0450.1
X-RAY DIFFRACTIONp_chiral_restr0.2111
X-RAY DIFFRACTIONp_singtor_nbd0.1851
X-RAY DIFFRACTIONp_multtor_nbd0.251
X-RAY DIFFRACTIONp_xhyhbond_nbd
X-RAY DIFFRACTIONp_xyhbond_nbd0.1941
X-RAY DIFFRACTIONp_planar_tor23.230
X-RAY DIFFRACTIONp_staggered_tor25.950
X-RAY DIFFRACTIONp_orthonormal_tor
X-RAY DIFFRACTIONp_transverse_tor35.150
X-RAY DIFFRACTIONp_special_tor
Software
*PLUS
Name: PROFFT / Classification: refinement
Refinement
*PLUS
Rfactor obs: 0.227
Solvent computation
*PLUS
Displacement parameters
*PLUS

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