3bch

Crystal Structure of the Human Laminin Receptor Precursor

Method: X-RAY DIFFRACTION Dmax: 61.6 Å Quality: GOOD

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

40S ribosomal protein SA

Homo sapiens

UniProt P08865

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 2–220 Fragment:laminin receptor precursor (UNP residues 2-220) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;290 K;pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.15 Å R-free 0.224

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.

192 other PDB entries and 197 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RSSA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 35–253; UniProt 2–220

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 3bch

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3bch
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3bch
Deposition date deposition_date2007-11-12
Structure title titleCrystal Structure of the Human Laminin Receptor Precursor
Keywords keywords;laminin receptor, p40 ribosomal protein, Acetylation, Cytoplasm, Phosphorylation, Polymorphism, Ribonucleoprotein, CELL ADHESION, RIBOSOMAL PROTEIN ;; CELL ADHESION, RIBOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.60
Radius of gyration Rg (electron density) rg_electron16.44
Forward intensity I(0) i08848030.00
Molecular weight molecular_weight22195.0 kDa
Excluded volume excluded_volume27944 ų
Envelope volume envelope_volume31536 ų
Hydration-shell volume shell_volume16069 ų
Envelope diameter envelope_diameter61.7
Shell Rg shell_rg22.53
Envelope Rg envelope_rg16.94
Shape Rg shape_rg16.45
Total Rg total_rg17.44
Total atoms total_atoms1563
Residues n_residues197
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 dmax61.6
Rg (real space) rg_real17.51
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real8.8480e+06
I(0) uncertainty (real space) i0_real_error9.8850e+04
Rg (reciprocal space) rg_reciprocal17.52
I(0) (reciprocal space) i0_reciprocal8848000.0000
Solution quality estimate total_estimate0.7796
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.325
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2527000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.717; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3bchA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10490 — Glucose-6-phosphate isomerase like protein; domain 1

8. Citations (1)

9. Files and Curves (10)