1eer

CRYSTAL STRUCTURE OF HUMAN ERYTHROPOIETIN COMPLEXED TO ITS RECEPTOR AT 1.9 ANGSTROMS

Method: X-RAY DIFFRACTION Dmax: 94.1 Å Quality: EXCELLENT

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

ERYTHROPOIETIN

Homo sapiens

UniProt P01588

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 28–193 Mutation:N24K, N38K, N83K, P121N, P122S ERYTHROPOIETIN RECEPTOR × 2 (P19235) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.50 Resolution 1.90 Å R-free 0.318

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EPO_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–166; UniProt 28–193

ERYTHROPOIETIN 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 31–250 Chain C; UniProt 31–250 Fragment:EXTRACELLULAR DOMAIN Mutation:N52Q, N164Q, A211E ERYTHROPOIETIN × 1 (P01588) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.50 Resolution 1.90 Å R-free 0.318

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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 8–227; UniProt 31–250 Author chain C; PDBConstruct 8–227; UniProt 31–250

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1eer

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1eer
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1eer
Deposition date deposition_date1998-07-24
Structure title titleCRYSTAL STRUCTURE OF HUMAN ERYTHROPOIETIN COMPLEXED TO ITS RECEPTOR AT 1.9 ANGSTROMS
Keywords keywords;ERYTHROPOIETIN, ERYTHROPOIETIN RECEPTOR, SIGNAL TRANSDUCTION, HEMATOPOIETIC CYTOKINE, CYTOKINE RECEPTOR CLASS 1, COMPLEX (CYTOKINE-RECEPTOR), COMPLEX (CYTOKINE-RECEPTOR) complex ;; COMPLEX (CYTOKINE/RECEPTOR)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.45
Radius of gyration Rg (electron density) rg_electron28.43
Forward intensity I(0) i069807500.00
Molecular weight molecular_weight65518.0 kDa
Excluded volume excluded_volume82041 ų
Envelope volume envelope_volume105450 ų
Hydration-shell volume shell_volume31227 ų
Envelope diameter envelope_diameter99.4
Shell Rg shell_rg35.30
Envelope Rg envelope_rg28.44
Shape Rg shape_rg28.44
Total Rg total_rg29.06
Total atoms total_atoms4619
Residues n_residues592
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax94.1
Rg (real space) rg_real29.40
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real6.9810e+07
I(0) uncertainty (real space) i0_real_error1.0060e+06
Rg (reciprocal space) rg_reciprocal29.42
I(0) (reciprocal space) i0_reciprocal69810000.0000
Solution quality estimate total_estimate0.9030
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.6
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.462
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11510000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.910

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd1eera_
Class classa — All alpha proteins
Fold Fold folda.26 — 4-helical cytokines
Superfamily Superfamily superfamilya.26.1 — 4-helical cytokines
Family Family familya.26.1.2 — Short-chain cytokines
Domain ID domain_idd1eerb1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III
Domain ID domain_idd1eerb2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III
Domain ID domain_idd1eerc1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III
Domain ID domain_idd1eerc2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III

CATH v4.4 (5 domains)

Domain ID domain_id1eerA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10
Domain ID domain_id1eerB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1eerB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1eerC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1eerC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)