2spm

A NOVEL SITE-DIRECTED MUTANT OF MYOGLOBIN WITH AN UNUSUALLY HIGH O2 AFFINITY AND LOW AUTOOXIDATION RATE

Method: X-RAY DIFFRACTION Dmax: 51.9 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 1–153 Not recorded SO4 SULFATE ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.70 Å

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_PHYCA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–154; 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 2spm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2spm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2spm
Deposition date deposition_date1993-08-25
Structure title titleA NOVEL SITE-DIRECTED MUTANT OF MYOGLOBIN WITH AN UNUSUALLY HIGH O2 AFFINITY AND LOW AUTOOXIDATION RATE
Keywords keywordsOXYGEN STORAGE; OXYGEN STORAGE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.62
Radius of gyration Rg (electron density) rg_electron15.19
Forward intensity I(0) i05809100.00
Molecular weight molecular_weight18080.0 kDa
Excluded volume excluded_volume22897 ų
Envelope volume envelope_volume25127 ų
Hydration-shell volume shell_volume14039 ų
Envelope diameter envelope_diameter51.0
Shell Rg shell_rg20.97
Envelope Rg envelope_rg15.38
Shape Rg shape_rg15.15
Total Rg total_rg16.38
Total atoms total_atoms1276
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 dmax51.9
Rg (real space) rg_real16.50
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real5.8090e+06
I(0) uncertainty (real space) i0_real_error6.6150e+04
Rg (reciprocal space) rg_reciprocal16.51
I(0) (reciprocal space) i0_reciprocal5809000.0000
Solution quality estimate total_estimate0.8207
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha871700.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2spma_
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_id2spmA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology490 — Globin-like
Homologous superfamily homologous superfamily10 — Globins

8. Citations (3)

9. Files and Curves (10)