1vyo

Crystal structure of avidin

Method: X-RAY DIFFRACTION Dmax: 66.6 Å Quality: EXCELLENT

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

AVIDIN

GALLUS GALLUS

UniProt P02701

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 25–152 Chain B; UniProt 25–152 Not recorded GOL GLYCEROL × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.6;295 K;Equal volumes (1 ul) of protein (0.5 mg/ml) in 50 mM Na acetate (pH 4) + 20 mM NaCl and well solution of 0.1 M MES (pH 6.6) + 24% PEG 8000 + 0.2 M Mg acetate Resolution 1.48 Å R-free 0.190

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.

35 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AVID_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–128; UniProt 25–152 Author chain B; PDBConstruct 1–128; UniProt 25–152

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 1vyo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1vyo
Deposition date deposition_date2004-05-03
Structure title titleCrystal structure of avidin
Keywords keywordsGLYCOPROTEIN, BIOTIN; GLYCOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.30
Radius of gyration Rg (electron density) rg_electron20.11
Forward intensity I(0) i014000900.00
Molecular weight molecular_weight27630.0 kDa
Excluded volume excluded_volume34425 ų
Envelope volume envelope_volume42966 ų
Hydration-shell volume shell_volume18098 ų
Envelope diameter envelope_diameter67.5
Shell Rg shell_rg25.89
Envelope Rg envelope_rg20.07
Shape Rg shape_rg20.09
Total Rg total_rg21.00
Total atoms total_atoms1941
Residues n_residues243
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 dmax66.6
Rg (real space) rg_real21.16
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real1.4000e+07
I(0) uncertainty (real space) i0_real_error1.6940e+05
Rg (reciprocal space) rg_reciprocal21.18
I(0) (reciprocal space) i0_reciprocal14000000.0000
Solution quality estimate total_estimate0.9018
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.3
Skewness Skewness skewness0.035
Kurtosis Kurtosis kurtosis-0.576
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2109000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.978

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_idd1vyoa_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd1vyob_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin

CATH v4.4 (2 domains)

Domain ID domain_id1vyoA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1vyoB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like

8. Citations (1)

9. Files and Curves (10)