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2n51

NMR structure of the C-terminal region of human eukaryotic elongation factor 1B

Method: SOLUTION NMR Dmax: 69.2 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Elongation factor 1-delta

Homo sapiens

UniProt P29692

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 153–281 Fragment：UNP RESIDUES 153-281 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7.5；298 K；Ionic strength (raw mmCIF value) 220；Pressure ambient NMR sample composition：0.8 mM [U-13C; U-15N] entity-1, 20 mM TRIS-2, 200 mM sodium chloride-3, 0.01 % w/v DSS-4, 90% H2O/10% D2O | 90% H2O/10% 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 2N51 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2MVM Solution structure of eEF1Bdelta CAR domain Deposited 2014-10-09 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 153–192（40 aa） Fragment：CAR domain (UNP residues 153-192)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.5；298 K；Pressure ambient
NMR sample composition 0.2-0.8 mM [U-13C; U-15N] eEF1Bdelta, 20 mM Tris, 200 mM sodium chloride, 0.01% DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2MVN Solution structure of eEF1Bdelta CAR domain in TCTP-bound state Deposited 2014-10-09 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 153–192（40 aa） Fragment：CAR domain (UNP residues 153-192)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.5；298 K；Pressure ambient
NMR sample composition 0.2-0.8 mM [U-13C; U-15N] eEF1Bdelta, 20 mM Tris, 200 mM sodium chloride, 0.01% DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
5JPO Complex structure of human elongation factor 1B gamma GST-liked domain and delta N-terminal domain Deposited 2016-05-04 Different construct 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 E 1–30（30 aa） Fragment：UNP RESIDUES 1-30
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

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

View Construct and Data Evidence
UniProt name EF1D_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 5–133； UniProt 153–281

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 2n51

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n51
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2n51
Deposition date deposition_date2015-07-02
Structure title titleNMR structure of the C-terminal region of human eukaryotic elongation factor 1B
Keywords keywordsGUANINE NUCLEOTIDE EXCHANGE FACTOR, TRANSLATION; TRANSLATION
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier25.83 Å
Radius of gyration Rg (electron density) rg_electron24.88 Å
Forward intensity I(0) i01293590000.00
Molecular weight molecular_weight297230.0 kDa
Excluded volume excluded_volume370220 ų
Envelope volume envelope_volume199720 ų
Hydration-shell volume shell_volume45101 ų
Envelope diameter envelope_diameter144.4 Å
Shell Rg shell_rg41.60 Å
Envelope Rg envelope_rg39.66 Å
Shape Rg shape_rg24.96 Å
Total Rg total_rg25.12 Å
Total atoms total_atoms41540
Residues n_residues2660
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 dmax69.2 Å
Rg (real space) rg_real23.42 Å
Rg uncertainty (real space) rg_real_error0.20 Å
I(0) (real space) i0_real1.2260e+09
I(0) uncertainty (real space) i0_real_error1.3560e+07
Rg (reciprocal space) rg_reciprocal26.34 Å
I(0) (reciprocal space) i0_reciprocal1293000000.0000
Solution quality estimate total_estimate0.6109
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.0 Å
Skewness Skewness skewness0.456
Kurtosis Kurtosis kurtosis-0.699
Angular range angular_range— – 0.3050 Å−1
Current regularization parameter α current_alpha2.0080
Highest regularization parameter α highest_alpha773800.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.839; Stabil: 0.981; Sysdev: 0.000; Positv: 1.000; Valcen: 0.540; 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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8. Citations (1)

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9. Files and Curves (10)