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- PDB-1ebp: COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ebp | ||||||
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Title | COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN AGONIST PEPTIDE [EMP1] | ||||||
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![]() | COMPLEX (CYTOKINE RECEPTOR/PEPTIDE) / ERYTHROPOIETIN RECEPTOR / SIGNAL TRANSDUCTION / PROTEIN MINIMIZATION / DRUG DESIGN / CYTOKINE RECEPTOR CLASS 1 / COMPLEX (CYTOKINE RECEPTOR-PEPTIDE) / COMPLEX (CYTOKINE RECEPTOR-PEPTIDE) complex | ||||||
Function / homology | ![]() erythropoietin receptor activity / Signaling by Erythropoietin / Erythropoietin activates STAT5 / Erythropoietin activates Phospholipase C gamma (PLCG) / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / hemopoiesis / decidualization / Erythropoietin activates RAS / brain development / cytokine-mediated signaling pathway ...erythropoietin receptor activity / Signaling by Erythropoietin / Erythropoietin activates STAT5 / Erythropoietin activates Phospholipase C gamma (PLCG) / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / hemopoiesis / decidualization / Erythropoietin activates RAS / brain development / cytokine-mediated signaling pathway / heart development / nuclear speck / external side of plasma membrane / positive regulation of cell population proliferation / signal transduction / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Livnah, O. / Stura, E.A. / Wilson, I.A. | ||||||
![]() | ![]() Title: Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 A. Authors: Livnah, O. / Stura, E.A. / Johnson, D.L. / Middleton, S.A. / Mulcahy, L.S. / Wrighton, N.C. / Dower, W.J. / Jolliffe, L.K. / Wilson, I.A. #1: ![]() Title: Small Peptides as Potent Mimetics of the Protein Hormone Erythropoietin Authors: Wrighton, N.C. / Farrell, F.X. / Chang, R. / Kashyap, A.K. / Barbone, F.P. / Mulcahy, L.S. / Johnson, D.L. / Barrett, R.W. / Jolliffe, L.K. / Dower, W.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 95 KB | Display | ![]() |
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PDB format | ![]() | 74.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 384.8 KB | Display | ![]() |
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Full document | ![]() | 407.5 KB | Display | |
Data in XML | ![]() | 12.6 KB | Display | |
Data in CIF | ![]() | 18.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 23327.467 Da / Num. of mol.: 2 / Fragment: EXTRACELLULAR DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 2097.376 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 57.65 % |
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Crystal grow | *PLUS Method: unknown |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 25 Å / Num. obs: 14158 / % possible obs: 93 % / Rmerge(I) obs: 0.05 |
Reflection shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 2.9 Å / % possible obs: 91 % |
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Processing
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Refinement | Resolution: 2.8→8 Å / σ(F): 1 Details: RESIDUES A 21 - A 23, B 21 - B 23, A 164 - A 166, B 133 - B 136 HAVE WEAK OR NO ELECTRON DENSITY AND WERE MODELED IN THE STRUCTURE. THESE RESIDUES HAVE OCCUPANCY 0.0 AND B VALUE OF 90.0.
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Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |