2o5m

Manganese horse heart myoglobin, azide modified

Method: X-RAY DIFFRACTION Dmax: 51.8 Å Quality: GOOD

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

Myoglobin

OrganismNot specified

UniProt P68082

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 X; UniProt 1–153 Not recorded AZI AZIDE ION × 1 SO4 SULFATE ION × 2 MNR PROTOPORPHYRIN IX CONTAINING MN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;296 K;Ammonium sulfate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 1.65 Å R-free 0.221

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.

149 other PDB entries and 156 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYG_HORSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 1–153; UniProt 1–153

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 2o5m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2o5m
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2o5m
Deposition date deposition_date2006-12-06
Structure title titleManganese horse heart myoglobin, azide modified
Keywords keywordsManganese myoglobin, manganese protoporphyrin IX, azide, horse heart, OXYGEN STORAGE-TRANSPORT COMPLEX; OXYGEN STORAGE/TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.59
Radius of gyration Rg (electron density) rg_electron15.11
Forward intensity I(0) i05796930.00
Molecular weight molecular_weight17727.0 kDa
Excluded volume excluded_volume22303 ų
Envelope volume envelope_volume24628 ų
Hydration-shell volume shell_volume13829 ų
Envelope diameter envelope_diameter51.6
Shell Rg shell_rg20.87
Envelope Rg envelope_rg15.37
Shape Rg shape_rg15.07
Total Rg total_rg16.28
Total atoms total_atoms1250
Residues n_residues152
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 dmax51.8
Rg (real space) rg_real16.48
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real5.7970e+06
I(0) uncertainty (real space) i0_real_error6.9020e+04
Rg (reciprocal space) rg_reciprocal16.49
I(0) (reciprocal space) i0_reciprocal5797000.0000
Solution quality estimate total_estimate0.8943
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.9
Skewness Skewness skewness0.114
Kurtosis Kurtosis kurtosis-0.461
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha902700.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.924

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2o5mx_
Class classa — All alpha proteins
Fold Fold folda.1 — Globin-like
Superfamily Superfamily superfamilya.1.1 — Globin-like
Family Family familya.1.1.2 — Globins

CATH v4.4 (1 domains)

Domain ID domain_id2o5mX00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology490 — Globin-like
Homologous superfamily homologous superfamily10 — Globins

8. Citations (1)

9. Files and Curves (10)