SAXSdb — 1cto

▼

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

GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR

Mus musculus

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 211–333	Fragment：C-TERMINAL DOMAIN OF THE LIGAND-BINDING REGION Mutation：INS(G1,S2,S3)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5.5；303 K	Resolution not provided

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 1CTO	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 method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 120–334（215 aa） Fragment：CRH REGION (BN DOMAIN:D1-108, BC DOMAIN:D109-215) Chain D 120–334（215 aa） Fragment：CRH REGION (BN DOMAIN:D1-108, BC DOMAIN:D109-215)	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
1GCF NMR STRUCTURE OF THE C-TERMINAL DOMAIN OF THE LIGAND-BINDING REGION OF MURINE GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR, 12 STRUCTURES Deposited 1997-04-10	Parsed fields agree	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 211–333（123 aa） Fragment：C-TERMINAL DOMAIN OF THE LIGAND-BINDING REGION	Mutation：INS(G1,S2,S3)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；303 K	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 method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 120–334（215 aa） Fragment：CRH REGION (BN DOMAIN:H1-108, BC DOMAIN:H109-215) Chain D 120–334（215 aa） Fragment：CRH REGION (BN DOMAIN:H1-108, BC DOMAIN:H109-215)	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 method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain F 120–334（215 aa） Fragment：CRH REGION (BN DOMAIN:H1-108, BC DOMAIN:H109-215) Chain H 120–334（215 aa） Fragment：CRH REGION (BN DOMAIN:H1-108, BC DOMAIN:H109-215)	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

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CSF3R_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–109； UniProt 211–333

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1cto
Deposition date deposition_date	1996-09-25
Structure title title	NMR STRUCTURE OF THE C-TERMINAL DOMAIN OF THE LIGAND-BINDING REGION OF MURINE GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR, MINIMIZED AVERAGE STRUCTURE
Keywords keywords	BINDING PROTEIN, CYTOKINE RECEPTOR; BINDING PROTEIN
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	16.16 Å
Radius of gyration Rg (electron density) rg_electron	15.04 Å
Forward intensity I(0) i0	3117500.00
Molecular weight molecular_weight	12525.0 kDa
Excluded volume excluded_volume	15757 Å³
Envelope volume envelope_volume	18956 Å³
Hydration-shell volume shell_volume	11270 Å³
Envelope diameter envelope_diameter	51.8 Å
Shell Rg shell_rg	19.92 Å
Envelope Rg envelope_rg	15.41 Å
Shape Rg shape_rg	15.02 Å
Total Rg total_rg	16.15 Å
Total atoms total_atoms	1739
Residues n_residues	109
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

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

Maximum dimension Dmax dmax	52.9 Å
Rg (real space) rg_real	16.13 Å
Rg uncertainty (real space) rg_real_error	0.24 Å
I(0) (real space) i0_real	3.1180e+06
I(0) uncertainty (real space) i0_real_error	3.8430e+04
Rg (reciprocal space) rg_reciprocal	16.13 Å
I(0) (reciprocal space) i0_reciprocal	3118000.0000
Solution quality estimate total_estimate	0.8949
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	18.1 Å
Skewness Skewness skewness	0.263
Kurtosis Kurtosis kurtosis	-0.419
Angular range angular_range	— – 0.4950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	599500.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.999

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1ctoa_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.2 — Fibronectin type III
Family Family family	b.1.2.1 — Fibronectin type III

CATH v4.4 (1 domains)

Domain ID domain_id	1ctoA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

▶

8. Citations (2)

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR
Molecular weight formula_weight	12536.5 kDa
Mutation mutation	INS(G1,S2,S3)
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1739

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

NMR STRUCTURE OF THE C-TERMINAL DOMAIN OF THE LIGAND-BINDING REGION OF MURINE GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR, MINIMIZED AVERAGE STRUCTURE

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

GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/ct/1cto/1cto.fit
pddf	/app/data/pr_computation/ct/1cto/1cto.pr.out
profile	/app/data/saxs_computation/ct/1cto/1cto.dat