6uiu

Artificial Iron Proteins: Modelling the Active Sites in Non-Heme Dioxygenases

Method: X-RAY DIFFRACTION Dmax: 55.5 Å Quality: GOOD

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

Streptavidin

Streptomyces avidinii

UniProt P22629

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 38–183 Mutation:K121A, E101Q, S112E QG7 N-(2-{bis[(pyridin-2-yl)methyl]amino}ethyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;295 K;26 mg/mL protein, 2.0 M ammonium sulfate, 0.1 M sodium acetate pH 4 Resolution 1.35 Å R-free 0.230

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.

312 other PDB entries and 368 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAV_STRAV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–159; UniProt 38–183

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 6uiu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6uiu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6uiu
Deposition date deposition_date2019-10-01
Structure title titleArtificial Iron Proteins: Modelling the Active Sites in Non-Heme Dioxygenases
Keywords keywordsBiotin binding artificial metalloprotein, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.11
Radius of gyration Rg (electron density) rg_electron14.96
Forward intensity I(0) i03905640.00
Molecular weight molecular_weight13549.0 kDa
Excluded volume excluded_volume16675 ų
Envelope volume envelope_volume19401 ų
Hydration-shell volume shell_volume11499 ų
Envelope diameter envelope_diameter54.0
Shell Rg shell_rg20.07
Envelope Rg envelope_rg15.64
Shape Rg shape_rg14.93
Total Rg total_rg16.01
Total atoms total_atoms960
Residues n_residues124
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 dmax55.5
Rg (real space) rg_real16.13
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real3.9060e+06
I(0) uncertainty (real space) i0_real_error4.5840e+04
Rg (reciprocal space) rg_reciprocal16.13
I(0) (reciprocal space) i0_reciprocal3906000.0000
Solution quality estimate total_estimate0.8682
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.3
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis-0.219
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha673300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.785; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.928; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6uiua1
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_idd6uiua2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id6uiuA00
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)