1rz4

Crystal Structure of Human eIF3k

Method: X-RAY DIFFRACTION Dmax: 66.0 Å Quality: GOOD

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

Eukaryotic translation initiation factor 3 subunit 11

Homo sapiens

UniProt Q9UBQ5

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 1–218 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;1.6M ammonium sulfate, 0.1M Hepes, 0.1M NaCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.10 Å R-free 0.222
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–218 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;1.6M ammonium sulfate, 0.1M Hepes, 0.1M NaCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.10 Å R-free 0.222

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.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF3C_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–218; UniProt 1–218

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 1rz4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1rz4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1rz4
Deposition date deposition_date2003-12-23
Structure title titleCrystal Structure of Human eIF3k
Keywords keywordsHEAT analogous motif, winged-helix, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.98
Radius of gyration Rg (electron density) rg_electron18.98
Forward intensity I(0) i011186900.00
Molecular weight molecular_weight24747.0 kDa
Excluded volume excluded_volume30800 ų
Envelope volume envelope_volume36357 ų
Hydration-shell volume shell_volume16623 ų
Envelope diameter envelope_diameter68.6
Shell Rg shell_rg24.50
Envelope Rg envelope_rg19.32
Shape Rg shape_rg18.98
Total Rg total_rg19.81
Total atoms total_atoms1718
Residues n_residues207
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 dmax66.0
Rg (real space) rg_real19.97
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.1190e+07
I(0) uncertainty (real space) i0_real_error1.4430e+05
Rg (reciprocal space) rg_reciprocal19.97
I(0) (reciprocal space) i0_reciprocal11190000.0000
Solution quality estimate total_estimate0.8059
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.336
Kurtosis Kurtosis kurtosis-0.364
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2103000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1rz4a1
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.47 — C-terminal part of PCI (proteasome COP9/signalosome eIF3) domains (PINT motif)
Domain ID domain_idd1rz4a2
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.8 — TPR-like
Family Family familya.118.8.9 — TPR-like repeats from PCI (proteasome / COP9 signalosome / eIF3) domains

CATH v4.4 (2 domains)

Domain ID domain_id1rz4A01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily250 — ARM repeat; domain 1
Domain ID domain_id1rz4A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

8. Citations (1)

9. Files and Curves (10)