9p1f

Myoglobin variant RR22 in complex with imidazole

Method: X-RAY DIFFRACTION Dmax: 51.9 Å Quality: REASONABLE

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

Myoglobin

Physeter macrocephalus

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 Mutation:V29, V33, V64, F68 IMD IMIDAZOLE × 1 SO4 SULFATE ION × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;20 mM Tris-HCl pH 8.8, 0.1 mM EDTA, 2.3 M Ammonium Sulfate Resolution 1.10 Å R-free 0.140

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 9p1f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9p1f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9p1f
Deposition date deposition_date2025-06-09
Structure title titleMyoglobin variant RR22 in complex with imidazole
Keywords keywordsMETALLOPROTEIN, MYOGLOBIN, HEME, OXYGEN STORAGE; OXYGEN STORAGE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.90
Radius of gyration Rg (electron density) rg_electron15.27
Forward intensity I(0) i06443140.00
Molecular weight molecular_weight18353.0 kDa
Excluded volume excluded_volume22923 ų
Envelope volume envelope_volume25675 ų
Hydration-shell volume shell_volume14190 ų
Envelope diameter envelope_diameter52.6
Shell Rg shell_rg21.21
Envelope Rg envelope_rg15.55
Shape Rg shape_rg15.19
Total Rg total_rg16.57
Total atoms total_atoms2550
Residues n_residues153
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 dmax51.9
Rg (real space) rg_real16.79
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real6.4430e+06
I(0) uncertainty (real space) i0_real_error7.9850e+04
Rg (reciprocal space) rg_reciprocal16.81
I(0) (reciprocal space) i0_reciprocal6443000.0000
Solution quality estimate total_estimate0.7474
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.099
Kurtosis Kurtosis kurtosis-0.474
Angular range angular_range— – 0.4700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha989900.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 0.322; Positv: 1.000; Valcen: 0.989; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)