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1rhg

THE STRUCTURE OF GRANULOCYTE-COLONY-STIMULATING FACTOR AND ITS RELATIONSHIP TO THOSE OF OTHER GROWTH FACTORS

Method: X-RAY DIFFRACTION Dmax: 82.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

GRANULOCYTE COLONY-STIMULATING FACTOR

Homo sapiens

UniProt P09919

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 31–207 Chain B； UniProt 31–207 Chain C； UniProt 31–207 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å

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 1RHG Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CD9 2:2 COMPLEX OF G-CSF WITH ITS RECEPTOR Deposited 1999-03-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 13–186（174 aa）
Chain C 13–186（174 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.50
Resolution 2.80 Å R-free 0.319
1GNC STRUCTURE AND DYNAMICS OF THE HUMAN GRANULOCYTE COLONY-STIMULATING FACTOR DETERMINED BY NMR SPECTROSCOPY. LOOP MOBILITY IN A FOUR-HELIX-BUNDLE PROTEIN Deposited 1994-03-08 Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 31–207（177 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1PGR 2:2 COMPLEX OF G-CSF WITH ITS RECEPTOR Deposited 1999-03-08 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 13–186（174 aa）
Chain C 13–186（174 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 3.50 Å
1PGR 2:2 COMPLEX OF G-CSF WITH ITS RECEPTOR Deposited 1999-03-08 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain E 13–186（174 aa）
Chain G 13–186（174 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 3.50 Å
2D9Q Crystal Structure of the Human GCSF-Receptor Signaling Complex Deposited 2005-12-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 31–204（174 aa） Fragment：residues 1-174
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.8；293 K；0.2M ammonium phosphate, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.80 Å R-free 0.284
5GW9 Crystal structure of C163, a backbone circularized G-CSF Deposited 2016-09-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 40–202（163 aa） Fragment：UNP residues 40-202
Mutation：P40S, C47S, A205G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293 K；0.4M Ammonium sulfate
Resolution 1.65 Å R-free 0.218
5GW9 Crystal structure of C163, a backbone circularized G-CSF Deposited 2016-09-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 40–202（163 aa） Fragment：UNP residues 40-202
Mutation：P40S, C47S, A205G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293 K；0.4M Ammonium sulfate
Resolution 1.65 Å R-free 0.218
5GW9 Crystal structure of C163, a backbone circularized G-CSF Deposited 2016-09-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 40–202（163 aa） Fragment：UNP residues 40-202
Mutation：P40S, C47S, A205G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293 K；0.4M Ammonium sulfate
Resolution 1.65 Å R-free 0.218
5GW9 Crystal structure of C163, a backbone circularized G-CSF Deposited 2016-09-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 40–202（163 aa） Fragment：UNP residues 40-202
Mutation：P40S, C47S, A205G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293 K；0.4M Ammonium sulfate
Resolution 1.65 Å R-free 0.218
5GW9 Crystal structure of C163, a backbone circularized G-CSF Deposited 2016-09-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 40–202（163 aa） Fragment：UNP residues 40-202
Chain C 40–202（163 aa） Fragment：UNP residues 40-202
Mutation：P40S, C47S, A205G Mutation：P40S, C47S, A205G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293 K；0.4M Ammonium sulfate
Resolution 1.65 Å R-free 0.218
5GW9 Crystal structure of C163, a backbone circularized G-CSF Deposited 2016-09-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 40–202（163 aa） Fragment：UNP residues 40-202
Chain D 40–202（163 aa） Fragment：UNP residues 40-202
Mutation：P40S, C47S, A205G Mutation：P40S, C47S, A205G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293 K；0.4M Ammonium sulfate
Resolution 1.65 Å R-free 0.218
5ZO6 Crystal structure of C166, a backbone circularized G-CSF Deposited 2018-04-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain X 37–205（169 aa） Fragment：UNP residues 37-205
Mutation：C11S, A166G No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；298 K；sodium acetate trihydrate, sodium chloride dehydrate, PEG 1500, MPD
Resolution 1.70 Å R-free 0.217

6 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSF3_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–174； UniProt 31–207 Author chain B； PDBConstruct 1–174； UniProt 31–207 Author chain C； PDBConstruct 1–174； UniProt 31–207

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 1rhg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1rhg
Deposition date deposition_date1993-01-29
Structure title titleTHE STRUCTURE OF GRANULOCYTE-COLONY-STIMULATING FACTOR AND ITS RELATIONSHIP TO THOSE OF OTHER GROWTH FACTORS
Keywords keywordsGROWTH FACTOR; GROWTH FACTOR
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier25.27 Å
Radius of gyration Rg (electron density) rg_electron24.59 Å
Forward intensity I(0) i034148200.00
Molecular weight molecular_weight46941.0 kDa
Excluded volume excluded_volume59613 ų
Envelope volume envelope_volume71739 ų
Hydration-shell volume shell_volume25145 ų
Envelope diameter envelope_diameter85.0 Å
Shell Rg shell_rg31.15 Å
Envelope Rg envelope_rg24.56 Å
Shape Rg shape_rg24.60 Å
Total Rg total_rg25.39 Å
Total atoms total_atoms3958
Residues n_residues434
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax82.7 Å
Rg (real space) rg_real25.30 Å
Rg uncertainty (real space) rg_real_error0.62 Å
I(0) (real space) i0_real3.4150e+07
I(0) uncertainty (real space) i0_real_error4.3790e+05
Rg (reciprocal space) rg_reciprocal25.29 Å
I(0) (reciprocal space) i0_reciprocal34150000.0000
Solution quality estimate total_estimate0.8875
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6 Å
Skewness Skewness skewness0.393
Kurtosis Kurtosis kurtosis-0.335
Angular range angular_range— – 0.3150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18600000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.981
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1rhga_
Class classa — All alpha proteins
Fold Fold folda.26 — 4-helical cytokines
Superfamily Superfamily superfamilya.26.1 — 4-helical cytokines
Family Family familya.26.1.1 — Long-chain cytokines
Domain ID domain_idd1rhgb_
Class classa — All alpha proteins
Fold Fold folda.26 — 4-helical cytokines
Superfamily Superfamily superfamilya.26.1 — 4-helical cytokines
Family Family familya.26.1.1 — Long-chain cytokines
Domain ID domain_idd1rhgc_
Class classa — All alpha proteins
Fold Fold folda.26 — 4-helical cytokines
Superfamily Superfamily superfamilya.26.1 — 4-helical cytokines
Family Family familya.26.1.1 — Long-chain cytokines

CATH v4.4 (3 domains)

Domain ID domain_id1rhgA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10 —
Domain ID domain_id1rhgB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10 —
Domain ID domain_id1rhgC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10 —
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8. Citations (4)

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9. Files and Curves (10)