SAXSdb — 1pbu

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

Elongation factor 1-gamma

Homo sapiens

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 276–437	Fragment：C-terminal domain (residues 276-437) Mutation：V289A	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 7.5；298 K；Ionic strength (raw mmCIF value) 75mM KCl；Pressure ambient NMR sample composition：1mM eEF1Bgamma[276-437]U-15N,13C, 20mM Tris-HCl pH7.5, 75mM KCl, 1mM DTT, 0.02%NaN3 (w/v) \| 95% H2O/5% D2O NMR sample composition：1mM eEF1Bgamma[276-437]U-15N, 20mM Tris-HCl pH7.5, 75mM KCl, 1mM DTT, 0.02%NaN3 (w/v) \| 95% H2O/5% D2O	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 1PBU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5DQS Complex structure of human elongation factor 1B alpha and gamma GST-like domains Deposited 2015-09-15	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–218（217 aa） Fragment：UNP RESIDUES 2-218	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；glycerol ethoxylate	Resolution 2.10 Å R-free 0.242
5JPO Complex structure of human elongation factor 1B gamma GST-liked domain and delta N-terminal domain Deposited 2016-05-04	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 × 10 PDB declaration: decameric	Chain A 1–218（218 aa） Fragment：UNP RESIDUES 1-218 Chain B 1–218（218 aa） Fragment：UNP RESIDUES 1-218 Chain C 1–218（218 aa） Fragment：UNP RESIDUES 1-218 Chain D 1–218（218 aa） Fragment：UNP RESIDUES 1-218	Not recorded	GOL GLYCEROL × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；SOKALAN CP7, KCl, HEPES	Resolution 2.00 Å R-free 0.203

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	EF1G_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–162； UniProt 276–437

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1pbu
Deposition date deposition_date	2003-05-15
Structure title title	Solution structure of the C-terminal domain of the human eEF1Bgamma subunit
Keywords keywords	ALPHA/BETA, TRANSLATION; TRANSLATION
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	16.11 Å
Radius of gyration Rg (electron density) rg_electron	15.42 Å
Forward intensity I(0) i0	1860390000.00
Molecular weight molecular_weight	380510.0 kDa
Excluded volume excluded_volume	479240 Å³
Envelope volume envelope_volume	35104 Å³
Hydration-shell volume shell_volume	17410 Å³
Envelope diameter envelope_diameter	57.4 Å
Shell Rg shell_rg	23.06 Å
Envelope Rg envelope_rg	16.92 Å
Shape Rg shape_rg	15.36 Å
Total Rg total_rg	15.73 Å
Total atoms total_atoms	52560
Residues n_residues	3240
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

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

Maximum dimension Dmax dmax	49.2 Å
Rg (real space) rg_real	15.99 Å
Rg uncertainty (real space) rg_real_error	0.24 Å
I(0) (real space) i0_real	1.8600e+09
I(0) uncertainty (real space) i0_real_error	1.8350e+07
Rg (reciprocal space) rg_reciprocal	16.00 Å
I(0) (reciprocal space) i0_reciprocal	1860000000.0000
Solution quality estimate total_estimate	0.8227
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.3 Å
Skewness Skewness skewness	0.067
Kurtosis Kurtosis kurtosis	-0.465
Angular range angular_range	— – 0.4950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	675300.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.905; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1pbua_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.46 — eEF1-gamma domain
Family Family family	d.58.46.1 — eEF1-gamma domain

CATH v4.4 (1 domains)

Domain ID domain_id	1pbuA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	1010 — Translation elongation factor EF1B, gamma chain, conserved domain

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8. Citations (1)

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Description description	Elongation factor 1-gamma
Molecular weight formula_weight	19066.3 kDa
Mutation mutation	V289A
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	52560

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

fit	/app/data/saxs_computation/pb/1pbu/1pbu.fit
pddf	/app/data/pr_computation/pb/1pbu/1pbu.pr.out
profile	/app/data/saxs_computation/pb/1pbu/1pbu.dat

Solution structure of the C-terminal domain of the human eEF1Bgamma subunit

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

Elongation factor 1-gamma

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

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 (1)

9. Files and Curves (10)

Files (7)

Curves (3)