SAXSdb — 1ebp

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1. Protein Identity and Related Structures Protein Identity & Related Structures

EPO RECEPTOR

Homo sapiens

UniProt P19235

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 34–244 Chain B； UniProt 34–244	Fragment：EXTRACELLULAR DOMAIN	EPO MIMETICS PEPTIDE 1 × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.80 Å R-free 0.334

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1EBP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CN4 ERYTHROPOIETIN COMPLEXED WITH EXTRACELLULAR DOMAINS OF ERYTHROPOIETIN RECEPTOR Deposited 1999-05-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 25–249（225 aa） Fragment：EXTRACELLULAR LIGAND BINDING DOMAINS Chain B 25–249（225 aa） Fragment：EXTRACELLULAR LIGAND BINDING DOMAINS	Mutation：N52Q, N164Q, A211E Mutation：N52Q, N164Q, A211E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.50	Resolution 2.80 Å R-free 0.336
1EBA COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY) Deposited 1998-10-02	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 34–248（215 aa） Fragment：EXTRACELLULAR DOMAIN Chain B 34–248（215 aa） Fragment：EXTRACELLULAR DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 2.70 Å R-free 0.299
1EBA COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY) Deposited 1998-10-02	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 34–248（215 aa） Fragment：EXTRACELLULAR DOMAIN Chain B 34–248（215 aa） Fragment：EXTRACELLULAR DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 2.70 Å R-free 0.299
1EBA COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY) Deposited 1998-10-02	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 34–248（215 aa） Fragment：EXTRACELLULAR DOMAIN Chain B 34–248（215 aa） Fragment：EXTRACELLULAR DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 2.70 Å R-free 0.299
1EER CRYSTAL STRUCTURE OF HUMAN ERYTHROPOIETIN COMPLEXED TO ITS RECEPTOR AT 1.9 ANGSTROMS Deposited 1998-07-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 31–250（220 aa） Fragment：EXTRACELLULAR DOMAIN Chain C 31–250（220 aa） Fragment：EXTRACELLULAR DOMAIN	Mutation：N52Q, N164Q, A211E Mutation：N52Q, N164Q, A211E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.50	Resolution 1.90 Å R-free 0.318
1ERN NATIVE STRUCTURE OF THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] Deposited 1999-01-11	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 34–246（213 aa） Fragment：EXTRACELLULAR DOMAIN Chain B 34–246（213 aa） Fragment：EXTRACELLULAR DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.7；pH 7.7	Resolution 2.40 Å R-free 0.295
2JIX Crystal structure of ABT-007 FAB fragment with the soluble domain of EPO receptor Deposited 2007-07-02	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 25–249（225 aa） Fragment：EPO RECEPTOR SOLUBLE DOMAIN, RESIDUES 25-249	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.20 Å R-free 0.323
2JIX Crystal structure of ABT-007 FAB fragment with the soluble domain of EPO receptor Deposited 2007-07-02	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 25–249（225 aa） Fragment：EPO RECEPTOR SOLUBLE DOMAIN, RESIDUES 25-249	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.20 Å R-free 0.323
2JIX Crystal structure of ABT-007 FAB fragment with the soluble domain of EPO receptor Deposited 2007-07-02	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 25–249（225 aa） Fragment：EPO RECEPTOR SOLUBLE DOMAIN, RESIDUES 25-249	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.20 Å R-free 0.323
2MV6 Solution structure of the transmembrane domain and the juxta-membrane domain of the Erythropoietin Receptor in micelles Deposited 2014-09-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 237–284（48 aa） Fragment：UNP residues 237-284	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；313 K；Ionic strength (raw mmCIF value) 20；Pressure ambient NMR sample composition 20 mM sodium phosphate, 10 v/v D2O, 250 mM DPC, 0.5 mM [U-99% 15N] protein, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5-1 mM [U-100% 13C; U-100% 15N] protein, 10 % D2O, 20 mM sodium phosphate, 200-400 mM DPC, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
4Y5V Diabody 305 complex with EpoR Deposited 2015-02-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 32–249（218 aa） Chain F 32–249（218 aa）	Mutation：N52Q, N164Q Mutation：N52Q, N164Q	GOL GLYCEROL × 10 PGE TRIETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；HEPES, PEG 4000	Resolution 2.60 Å R-free 0.229
4Y5V Diabody 305 complex with EpoR Deposited 2015-02-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain I 32–249（218 aa）	Mutation：N52Q, N164Q	GOL GLYCEROL × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；HEPES, PEG 4000	Resolution 2.60 Å R-free 0.229
4Y5X Diabody 305 complex with EpoR Deposited 2015-02-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 32–249（218 aa） Chain L 32–249（218 aa）	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 12 FLC CITRATE ANION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；293 K；sodium citrate, PEG 8000	Resolution 3.15 Å R-free 0.241
4Y5X Diabody 305 complex with EpoR Deposited 2015-02-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain F 32–249（218 aa） Chain I 32–249（218 aa）	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；293 K；sodium citrate, PEG 8000	Resolution 3.15 Å R-free 0.241
4Y5Y Diabody 330 complex with EpoR Deposited 2015-02-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 32–249（218 aa） Chain F 32–249（218 aa）	Mutation：N76Q, N188Q, D247L, and L248D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：N76Q, N188Q, D247L, and L248D Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；293 K；Magnesium chloride, Tris, PEG 8000	Resolution 2.85 Å R-free 0.241
6E2Q Structure of human JAK2 FERM/SH2 in complex with Erythropoietin Receptor Deposited 2018-07-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain N 273–338（66 aa） Fragment：UNP residues 273-338	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；277.15 K；100 mM Tris, pH 7.6, 2-4% PEG8000	Resolution 2.65 Å R-free 0.263
6E2Q Structure of human JAK2 FERM/SH2 in complex with Erythropoietin Receptor Deposited 2018-07-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain O 273–338（66 aa） Fragment：UNP residues 273-338	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；277.15 K；100 mM Tris, pH 7.6, 2-4% PEG8000	Resolution 2.65 Å R-free 0.263
6E2Q Structure of human JAK2 FERM/SH2 in complex with Erythropoietin Receptor Deposited 2018-07-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain M 273–338（66 aa） Fragment：UNP residues 273-338	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；277.15 K；100 mM Tris, pH 7.6, 2-4% PEG8000	Resolution 2.65 Å R-free 0.263
6E2Q Structure of human JAK2 FERM/SH2 in complex with Erythropoietin Receptor Deposited 2018-07-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 273–338（66 aa） Fragment：UNP residues 273-338	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；277.15 K；100 mM Tris, pH 7.6, 2-4% PEG8000	Resolution 2.65 Å R-free 0.263
6MOE Monomeric DARPin E2 complex with EpoR Deposited 2018-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 32–249（218 aa）	Not recorded	PO4 PHOSPHATE ION × 5 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.6；295 K；1 M sodium potassium phosphate pH 5.6 Cryoprotected in 25% ethylene glycol	Resolution 2.09 Å R-free 0.230
6MOE Monomeric DARPin E2 complex with EpoR Deposited 2018-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 32–249（218 aa）	Not recorded	PO4 PHOSPHATE ION × 4 EDO 1,2-ETHANEDIOL × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.6；295 K；1 M sodium potassium phosphate pH 5.6 Cryoprotected in 25% ethylene glycol	Resolution 2.09 Å R-free 0.230
6MOF Monomeric DARPin G2 complex with EpoR Deposited 2018-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 32–249（218 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；295 K；0.2 M Magnesium chloride, 0.1 M Tris pH 7.0, 10% PEG 8000, 25% ethylene glycol as cryoprotectant	Resolution 2.89 Å R-free 0.266
6MOH Dimeric DARPin C_R3 complex with EpoR Deposited 2018-10-04	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 32–249（218 aa） Chain D 32–249（218 aa）	Not recorded	PO4 PHOSPHATE ION × 7 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.3；295 K；0.1 M HEPES pH 7.3, 1.4 M sodium potassium phosphate, 24% glycerol cryoprotectant	Resolution 3.20 Å R-free 0.277
6MOI Dimeric DARPin C_angle_R5 complex with EpoR Deposited 2018-10-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 32–249（218 aa）	Not recorded	SO4 SULFATE ION × 4 EDO 1,2-ETHANEDIOL × 20 MG MAGNESIUM ION × 4 PEG DI(HYDROXYETHYL)ETHER × 2 PGE TRIETHYLENE GLYCOL × 2 PG4 TETRAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；295 K；0.3 M magnesium sulfate, 0.1 M bis-tris propane pH 7, 22.5% PurePEGs cocktail (Anatrace), 30% ethylene glycol cryoprotectant	Resolution 2.06 Å R-free 0.251
6MOJ Dimeric DARPin A_angle_R5 complex with EpoR Deposited 2018-10-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 32–249（218 aa）	Not recorded	TAR D(-)-TARTARIC ACID × 6 GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.2 M sodium potassium tartrate, 0.1 M bis-tris propane pH 8.5, 20% PEG 3350, 30% glycerol as cryoprotectant	Resolution 2.43 Å R-free 0.250
6MOK Dimeric DARPin A_distance_R7 complex with EpoR Deposited 2018-10-04	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 32–249（218 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.2 M NaCl, 0.1 M Tris pH 8.5, 25% PEG 3350	Resolution 5.10 Å R-free 0.299
6MOL Monoextended DARPin M_R12 complex with EpoR Deposited 2018-10-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 32–249（218 aa） Chain C 32–249（218 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；Seeded from 0.2 M NaCl, 0.1 M CAPS pH 10.5, 20% PEG 8000 into 0.2 M ammonium tartrate and 20% PEG 3350, with 10% glycerol, 10% ethylene glycol as cryoprotectant	Resolution 3.16 Å R-free 0.260
8VUI Structure of FabS1CE-EPR-1, an elbow-locked Fab, in complex with the erythropoeitin receptor Deposited 2024-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 25–250（226 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 3 NA SODIUM ION × 4 CL CHLORIDE ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CIT CITRIC ACID × 1 NH4 AMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.2；298 K；0.2 M Ammonium Citrate dibasic, 20% PEG2000 monomethyl ether, pH 5.2	Resolution 2.10 Å R-free 0.240
8VVM Structure of FabS1CE1-EPR1-1 in complex with the erythropoietin receptor Deposited 2024-01-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 25–250（226 aa）	Mutation：residues 22-250	PEG DI(HYDROXYETHYL)ETHER × 2 NA SODIUM ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；0.1 M MMT buffer pH 5.0, 25% PEG1500	Resolution 2.90 Å R-free 0.273
8VVO Structure of FabS1CE2-EPR1-1 in complex with the erythropoietin receptor Deposited 2024-01-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 25–250（226 aa）	Mutation：residues 22-250	NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；0.1 M MMT buffer pH 6.0, 25% PEG1500	Resolution 3.09 Å R-free 0.289

20 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	EPOR_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–211； UniProt 34–244 Author chain B； PDBConstruct 1–211； UniProt 34–244

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1ebp
Deposition date deposition_date	1996-05-07
Structure title title	COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN AGONIST PEPTIDE [EMP1]
Keywords keywords	;ERYTHROPOIETIN RECEPTOR, SIGNAL TRANSDUCTION, PROTEIN MINIMIZATION, DRUG DESIGN, CYTOKINE RECEPTOR CLASS 1, COMPLEX (CYTOKINE RECEPTOR-PEPTIDE), COMPLEX (CYTOKINE RECEPTOR-PEPTIDE) complex ;; COMPLEX (CYTOKINE RECEPTOR/PEPTIDE)
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	29.65 Å
Radius of gyration Rg (electron density) rg_electron	28.96 Å
Forward intensity I(0) i0	42104900.00
Molecular weight molecular_weight	50263.0 kDa
Excluded volume excluded_volume	62872 Å³
Envelope volume envelope_volume	87138 Å³
Hydration-shell volume shell_volume	26355 Å³
Envelope diameter envelope_diameter	105.3 Å
Shell Rg shell_rg	34.48 Å
Envelope Rg envelope_rg	29.10 Å
Shape Rg shape_rg	28.96 Å
Total Rg total_rg	29.56 Å
Total atoms total_atoms	3546
Residues n_residues	454
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	95.7 Å
Rg (real space) rg_real	29.71 Å
Rg uncertainty (real space) rg_real_error	0.87 Å
I(0) (real space) i0_real	4.2100e+07
I(0) uncertainty (real space) i0_real_error	7.3680e+05
Rg (reciprocal space) rg_reciprocal	29.69 Å
I(0) (reciprocal space) i0_reciprocal	42100000.0000
Solution quality estimate total_estimate	0.8982
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	36.1 Å
Skewness Skewness skewness	0.330
Kurtosis Kurtosis kurtosis	-0.422
Angular range angular_range	— – 0.2650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3834000.0000
Real-space data points n_real_points	54
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.880

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	EPO RECEPTOR
Molecular weight formula_weight	23327.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3546

KFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGNYSFSYQLEDEPWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLDAPVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGNGAGSVQRVEILEGRTECVLSNLRGRTRYTFAVRARMAEPSFGGFWSAWSEPVSLLT

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	EPO MIMETICS PEPTIDE 1
Molecular weight formula_weight	2097.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

GGTYSCHFGPLTWVCKPQGG

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7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1ebpa1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.2 — Fibronectin type III
Family Family family	b.1.2.1 — Fibronectin type III

Domain ID domain_id	d1ebpa2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.2 — Fibronectin type III
Family Family family	b.1.2.1 — Fibronectin type III

Domain ID domain_id	d1ebpb1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.2 — Fibronectin type III
Family Family family	b.1.2.1 — Fibronectin type III

Domain ID domain_id	d1ebpb2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.2 — Fibronectin type III
Family Family family	b.1.2.1 — Fibronectin type III

Domain ID domain_id	d1ebpc_
Class class	k — Designed proteins
Fold Fold fold	k.18 — Erythropoietin (EPO) mimetic peptides
Superfamily Superfamily superfamily	k.18.1 — Erythropoietin (EPO) mimetic peptides
Family Family family	k.18.1.1 — Erythropoietin (EPO) mimetic peptides

Domain ID domain_id	d1ebpd_
Class class	k — Designed proteins
Fold Fold fold	k.18 — Erythropoietin (EPO) mimetic peptides
Superfamily Superfamily superfamily	k.18.1 — Erythropoietin (EPO) mimetic peptides
Family Family family	k.18.1.1 — Erythropoietin (EPO) mimetic peptides

CATH v4.4 (4 domains)

Domain ID domain_id	1ebpA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1ebpA02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1ebpB01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	1ebpB02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (2)

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Unit-cell length a length_a	59.240 Å
Unit-cell length b length_b	75.500 Å
Unit-cell length c length_c	132.180 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2100
R_work r_work	0.2100
R_free r_free	0.3340

fit	/app/data/saxs_computation/eb/1ebp/1ebp.fit
pddf	/app/data/pr_computation/eb/1ebp/1ebp.pr.out
profile	/app/data/saxs_computation/eb/1ebp/1ebp.dat

COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN AGONIST PEPTIDE [EMP1]

1. Protein Identity and Related Structures Protein Identity & Related Structures

EPO RECEPTOR

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

CATH v4.4 (4 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)