4wrm

Structure of the human CSF-1:CSF-1R complex

Method: X-RAY DIFFRACTION Dmax: 153.5 Å Quality: REASONABLE

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

Macrophage colony-stimulating factor 1 receptor

Homo sapiens

UniProt P07333

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 20–504 Fragment:UNP RESIDUES 20-504 Macrophage colony-stimulating factor 1 × 1 (P09603) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1 M NaCl, 0.1 M Tris pH 8.0 and 8% w/v PEG 20000 Resolution 6.85 Å R-free 0.359

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.

25 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSF1R_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–485; UniProt 20–504

Macrophage colony-stimulating factor 1

Homo sapiens

UniProt P09603

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 33–181 Fragment:UNP RESIDUES 33-181 Macrophage colony-stimulating factor 1 receptor × 1 (P07333) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1 M NaCl, 0.1 M Tris pH 8.0 and 8% w/v PEG 20000 Resolution 6.85 Å R-free 0.359

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.

7 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSF1_HUMAN
Isoform P09603-3
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 22–170; UniProt 33–181

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 4wrm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4wrm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4wrm
Deposition date deposition_date2014-10-24
Structure title titleStructure of the human CSF-1:CSF-1R complex
Keywords keywordscytokine-cytokine receptor complex; CYTOKINE/CYTOKINE RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.50
Radius of gyration Rg (electron density) rg_electron44.78
Forward intensity I(0) i063956900.00
Molecular weight molecular_weight64209.0 kDa
Excluded volume excluded_volume80153 ų
Envelope volume envelope_volume125570 ų
Hydration-shell volume shell_volume26645 ų
Envelope diameter envelope_diameter152.8
Shell Rg shell_rg42.45
Envelope Rg envelope_rg43.99
Shape Rg shape_rg44.82
Total Rg total_rg44.50
Total atoms total_atoms4524
Residues n_residues586
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 dmax153.5
Rg (real space) rg_real44.20
Rg uncertainty (real space) rg_real_error2.23
I(0) (real space) i0_real6.3960e+07
I(0) uncertainty (real space) i0_real_error1.2200e+06
Rg (reciprocal space) rg_reciprocal43.51
I(0) (reciprocal space) i0_reciprocal63910000.0000
Solution quality estimate total_estimate0.6604
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.502
Kurtosis Kurtosis kurtosis-0.697
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2426000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.463; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.194; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)