5iru

Crystal structure of avidin in complex with 1-biotinylpyrene

Method: X-RAY DIFFRACTION Dmax: 71.2 Å Quality: EXCELLENT

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

Avidin

OrganismNot specified

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 Chain C; UniProt 25–152 Chain D; UniProt 25–152 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 B9P 1-biotinylpyrene × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;292.15 K;28% w/v polyethylene glycol monomethyl ether 2000, 0.1 M Bis-Tris, 0.1 M trimethylamine hydrochloride Resolution 2.00 Å R-free 0.265

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 Author chain C; PDBConstruct 1–128; UniProt 25–152 Author chain D; 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 5iru

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5iru
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5iru
Deposition date deposition_date2016-03-14
Structure title titleCrystal structure of avidin in complex with 1-biotinylpyrene
Keywords keywordscomplex, biotin binding protein; biotin binding protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.33
Radius of gyration Rg (electron density) rg_electron21.95
Forward intensity I(0) i054539600.00
Molecular weight molecular_weight56953.0 kDa
Excluded volume excluded_volume71022 ų
Envelope volume envelope_volume82027 ų
Hydration-shell volume shell_volume29492 ų
Envelope diameter envelope_diameter75.2
Shell Rg shell_rg30.19
Envelope Rg envelope_rg22.44
Shape Rg shape_rg21.91
Total Rg total_rg23.01
Total atoms total_atoms4008
Residues n_residues488
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 dmax71.2
Rg (real space) rg_real23.15
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real5.4540e+07
I(0) uncertainty (real space) i0_real_error6.7720e+05
Rg (reciprocal space) rg_reciprocal23.19
I(0) (reciprocal space) i0_reciprocal54540000.0000
Solution quality estimate total_estimate0.9021
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.7
Skewness Skewness skewness0.080
Kurtosis Kurtosis kurtosis-0.534
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19520000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5irua_
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_idd5irub_
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_idd5iruc_
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_idd5irud_
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 (4 domains)

Domain ID domain_id5iruA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5iruB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5iruC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5iruD00
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)