5myq

Crystal structure of avidin in complex with ferrocene homobiotin derivative

Method: X-RAY DIFFRACTION Dmax: 67.0 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 HBF ferrocene homobiotin derivative × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 IOD IODIDE ION × 21 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;292.15 K;0.2 M ammonium iodide, 22 % w/v PEG 3350 Resolution 1.89 Å R-free 0.232

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 5myq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5myq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5myq
Deposition date deposition_date2017-01-27
Structure title titleCrystal structure of avidin in complex with ferrocene homobiotin derivative
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_guinier23.29
Radius of gyration Rg (electron density) rg_electron21.93
Forward intensity I(0) i068914000.00
Molecular weight molecular_weight59509.0 kDa
Excluded volume excluded_volume71335 ų
Envelope volume envelope_volume80997 ų
Hydration-shell volume shell_volume29343 ų
Envelope diameter envelope_diameter70.2
Shell Rg shell_rg29.92
Envelope Rg envelope_rg22.17
Shape Rg shape_rg21.80
Total Rg total_rg23.06
Total atoms total_atoms4009
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 dmax67.0
Rg (real space) rg_real23.10
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real6.8910e+07
I(0) uncertainty (real space) i0_real_error7.6840e+05
Rg (reciprocal space) rg_reciprocal23.14
I(0) (reciprocal space) i0_reciprocal68920000.0000
Solution quality estimate total_estimate0.9139
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.9
Skewness Skewness skewness0.043
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14610000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.967; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5myqa_
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_idd5myqb_
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_idd5myqc_
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_idd5myqd_
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_id5myqA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5myqB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5myqC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5myqD00
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)