1d7q

HUMAN TRANSLATION INITIATION FACTOR EIF1A

Method: SOLUTION NMR Dmax: 71.9 Å Quality: REASONABLE

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

TRANSLATION INITIATION FACTOR 1A

Homo sapiens

UniProt P47813

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–143 Not recorded PROTEIN (N-TERMINAL HISTIDINE TAG) × 1 SOLUTION NMR NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 500mM;Pressure 1 NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 500mM;Pressure 1 NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 500mM;Pressure 1 NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 500mM;Pressure 1 NMR sample composition:0.8MM U-13C,15N EIF1A, 10MM PHOSPHATE BUFFER, PH 7.5, 500MM NACL, 1MM DTT, 0.1MM EDTA NMR sample composition:0.5MM U-15N EIF1A, 10MM PHOSPHATE BUFFER, PH 7.5, 500MM NACL, 1MM DTT, 0.1MM EDTA NMR sample composition:1.2MM EIF1A, 10MM PHOSPHATE BUFFER, PH 7.5, 500MM NACL, 1MM DTT, 0.1MM EDTA NMR sample composition:0.4MM 15N-LYSINE EIF1A, 10MM PHOSPHATE BUFFER, PH 7.5, 500MM NACL, 1MM DTT, 0.1MM EDTA 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF1AX_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–143; UniProt 1–143

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 1d7q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1d7q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1d7q
Deposition date deposition_date1999-10-19
Structure title titleHUMAN TRANSLATION INITIATION FACTOR EIF1A
Keywords keywordsOB-FOLD, BETA-BARREL, RNA-BINDING PROTEIN, GENE REGULATION; GENE REGULATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier27.16
Radius of gyration Rg (electron density) rg_electron26.11
Forward intensity I(0) i02125460000.00
Molecular weight molecular_weight360460.0 kDa
Excluded volume excluded_volume440500 ų
Envelope volume envelope_volume255030 ų
Hydration-shell volume shell_volume54897 ų
Envelope diameter envelope_diameter147.1
Shell Rg shell_rg44.06
Envelope Rg envelope_rg39.66
Shape Rg shape_rg26.13
Total Rg total_rg26.59
Total atoms total_atoms49920
Residues n_residues3140
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 dmax71.9
Rg (real space) rg_real25.37
Rg uncertainty (real space) rg_real_error0.19
I(0) (real space) i0_real2.0200e+09
I(0) uncertainty (real space) i0_real_error2.4930e+07
Rg (reciprocal space) rg_reciprocal27.49
I(0) (reciprocal space) i0_reciprocal2125000000.0000
Solution quality estimate total_estimate0.6618
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.325
Kurtosis Kurtosis kurtosis-0.772
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha2.7600
Highest regularization parameter α highest_alpha2307000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.961; Stabil: 0.980; Sysdev: 0.000; Positv: 1.000; Valcen: 0.784; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1d7qa_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.5 — Cold shock DNA-binding domain-like

CATH v4.4 (1 domains)

Domain ID domain_id1d7qA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins

8. Citations (2)

9. Files and Curves (10)