2bb2

X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS

Method: X-RAY DIFFRACTION Dmax: 76.8 Å Quality: REASONABLE

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

BETA B2-CRYSTALLIN

Bos taurus

UniProt P02522

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 14–194 Not recorded BME BETA-MERCAPTOETHANOL × 8 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.10 Å
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 14–194 Not recorded BME BETA-MERCAPTOETHANOL × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.10 Å

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.

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

View Construct and Data Evidence
UniProt name CRBB2_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–181; UniProt 14–194

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 2bb2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bb2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bb2
Deposition date deposition_date1992-09-21
Structure title titleX-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS
Keywords keywordsEYE LENS PROTEIN; EYE LENS PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.28
Radius of gyration Rg (electron density) rg_electron24.59
Forward intensity I(0) i07857090.00
Molecular weight molecular_weight20851.0 kDa
Excluded volume excluded_volume25827 ų
Envelope volume envelope_volume33608 ų
Hydration-shell volume shell_volume11995 ų
Envelope diameter envelope_diameter75.9
Shell Rg shell_rg30.12
Envelope Rg envelope_rg23.72
Shape Rg shape_rg24.59
Total Rg total_rg25.25
Total atoms total_atoms1472
Residues n_residues176
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 dmax76.8
Rg (real space) rg_real25.47
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real7.8570e+06
I(0) uncertainty (real space) i0_real_error1.1250e+05
Rg (reciprocal space) rg_reciprocal25.42
I(0) (reciprocal space) i0_reciprocal7857000.0000
Solution quality estimate total_estimate0.6723
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.3
Skewness Skewness skewness0.232
Kurtosis Kurtosis kurtosis-1.195
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1550000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.174; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.299; Smooth: 0.915

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_idd2bb2a1
Class classb — All beta proteins
Fold Fold foldb.11 — gamma-Crystallin-like
Superfamily Superfamily superfamilyb.11.1 — gamma-Crystallin-like
Family Family familyb.11.1.1 — Crystallins/Ca-binding development proteins
Domain ID domain_idd2bb2a2
Class classb — All beta proteins
Fold Fold foldb.11 — gamma-Crystallin-like
Superfamily Superfamily superfamilyb.11.1 — gamma-Crystallin-like
Family Family familyb.11.1.1 — Crystallins/Ca-binding development proteins

CATH v4.4 (2 domains)

Domain ID domain_id2bb2A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology20 — Gamma-B Crystallin; domain 1
Homologous superfamily homologous superfamily10 — Crystallins
Domain ID domain_id2bb2A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology20 — Gamma-B Crystallin; domain 1
Homologous superfamily homologous superfamily10 — Crystallins

8. Citations (2)

9. Files and Curves (10)