2gmf

HUMAN GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR

Method: X-RAY DIFFRACTION Dmax: 71.8 Å Quality: EXCELLENT

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

GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR

Homo sapiens

UniProt P04141

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 18–144 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 18–144 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.40 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.

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

View Construct and Data Evidence
UniProt name CSF2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–127; UniProt 18–144 Author chain B; PDBConstruct 1–127; UniProt 18–144

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 2gmf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2gmf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2gmf
Deposition date deposition_date1996-04-24
Structure title titleHUMAN GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR
Keywords keywordsGRANULOCYTE-MACROPHAGE COLONY STIMULATING GROWTH FACTOR, GROWTH FACTOR; GROWTH FACTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.28
Radius of gyration Rg (electron density) rg_electron21.41
Forward intensity I(0) i013814900.00
Molecular weight molecular_weight27625.0 kDa
Excluded volume excluded_volume34471 ų
Envelope volume envelope_volume42704 ų
Hydration-shell volume shell_volume17416 ų
Envelope diameter envelope_diameter71.7
Shell Rg shell_rg26.71
Envelope Rg envelope_rg21.45
Shape Rg shape_rg21.41
Total Rg total_rg22.17
Total atoms total_atoms1935
Residues n_residues241
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 dmax71.8
Rg (real space) rg_real22.30
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.3810e+07
I(0) uncertainty (real space) i0_real_error1.6830e+05
Rg (reciprocal space) rg_reciprocal22.30
I(0) (reciprocal space) i0_reciprocal13810000.0000
Solution quality estimate total_estimate0.9052
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.302
Kurtosis Kurtosis kurtosis-0.548
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha2232000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2gmfa1
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_idd2gmfa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2gmfb1
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_idd2gmfb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id2gmfA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10
Domain ID domain_id2gmfB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10

8. Citations (3)

9. Files and Curves (10)