9dti

F33Y CuBMb

Method: X-RAY DIFFRACTION Dmax: 50.7 Å Quality: GOOD

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

Myoglobin

Physeter catodon

UniProt P02185

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–154 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;F33Y CuBMb (2.2 mM) in 20 mM tris(hydroxymethyl)aminomethane (tris) pH 8 (pH adjusted H2SO4), was mixed 1:1 with well buffer (0.2 M sodium acetate, 0.1 M tris hydrochloride pH 8.5, with 30% polyethylene glycol 4000) using the hanging drop method, with 300 uL well buffer in the well of the crystallization tray, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.68 Å R-free 0.192

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.

354 other PDB entries and 366 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYG_PHYMC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–154; UniProt 1–154

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 9dti

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9dti
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9dti
Deposition date deposition_date2024-10-01
Structure title titleF33Y CuBMb
Keywords keywordsoxidase, metalloenzyme, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.50
Radius of gyration Rg (electron density) rg_electron15.13
Forward intensity I(0) i06061210.00
Molecular weight molecular_weight18217.0 kDa
Excluded volume excluded_volume22958 ų
Envelope volume envelope_volume25043 ų
Hydration-shell volume shell_volume14005 ų
Envelope diameter envelope_diameter49.3
Shell Rg shell_rg21.00
Envelope Rg envelope_rg15.33
Shape Rg shape_rg15.11
Total Rg total_rg16.29
Total atoms total_atoms1293
Residues n_residues154
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 dmax50.7
Rg (real space) rg_real16.38
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real6.0610e+06
I(0) uncertainty (real space) i0_real_error5.9880e+04
Rg (reciprocal space) rg_reciprocal16.39
I(0) (reciprocal space) i0_reciprocal6061000.0000
Solution quality estimate total_estimate0.8263
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.1
Skewness Skewness skewness0.096
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1044000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)