5lxf

Crystal structure of the human Macrophage Colony Stimulating Factor M- CSF_C31S variant

Method: X-RAY DIFFRACTION Dmax: 85.0 Å Quality: GOOD

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

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 33–190 Chain B; UniProt 33–190 Mutation:C31S No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.8;293 K;0.03M Bis-Tris pH 6.5; 0.17M Mg Formate; 16.67% PEG 3350; 0.07M Bis-Tris pH 5.5 Resolution 2.00 Å R-free 0.253

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 1
Chains and sequence ranges Author chain A; PDBConstruct 13–170; UniProt 33–190 Author chain B; PDBConstruct 13–170; UniProt 33–190

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 5lxf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5lxf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5lxf
Deposition date deposition_date2016-09-21
Structure title titleCrystal structure of the human Macrophage Colony Stimulating Factor M- CSF_C31S variant
Keywords keywordsDrug design, rational protein engineering, receptor tyrosine kinase, osteoporosis, signaling protein; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.59
Radius of gyration Rg (electron density) rg_electron24.90
Forward intensity I(0) i021311300.00
Molecular weight molecular_weight34375.0 kDa
Excluded volume excluded_volume42726 ų
Envelope volume envelope_volume52175 ų
Hydration-shell volume shell_volume19328 ų
Envelope diameter envelope_diameter86.7
Shell Rg shell_rg29.73
Envelope Rg envelope_rg25.12
Shape Rg shape_rg24.91
Total Rg total_rg25.50
Total atoms total_atoms2407
Residues n_residues295
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 dmax85.0
Rg (real space) rg_real25.86
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real2.1310e+07
I(0) uncertainty (real space) i0_real_error3.1860e+05
Rg (reciprocal space) rg_reciprocal25.77
I(0) (reciprocal space) i0_reciprocal21310000.0000
Solution quality estimate total_estimate0.8363
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.555
Kurtosis Kurtosis kurtosis-0.427
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2883000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.745; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.718; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5lxfa_
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_idd5lxfb_
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

CATH v4.4 (2 domains)

Domain ID domain_id5lxfA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10
Domain ID domain_id5lxfB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)