3h57

Myoglobin Cavity Mutant H64LV68N Deoxy form

Method: X-RAY DIFFRACTION Dmax: 50.1 Å Quality: REASONABLE

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 Mutation:H64L, V68N, D122N HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:Batch Method;pH 9;293 K;Protein Solution (20mg/ml protein in 0.02M Tris.HCl pH9.0) mixed with mother liquor (3.2M Ammonium Sulphate, 0.05M Tris.HCl, pH9.0) for final concentrations of 2.5M Ammonium Sulphate, Batch Method, temperature 293K Resolution 1.70 Å R-free 0.233

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 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 3h57

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3h57
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3h57
Deposition date deposition_date2009-04-21
Structure title titleMyoglobin Cavity Mutant H64LV68N Deoxy form
Keywords keywords;Myoglobin, active site hydration, ligand entry and exit, oxygen storage and transport, Heme, Iron, Metal-binding, Muscle protein, Oxygen transport, Transport, OXYGEN STORAGE ;; OXYGEN STORAGE, OXYGEN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.38
Radius of gyration Rg (electron density) rg_electron15.03
Forward intensity I(0) i05583920.00
Molecular weight molecular_weight17924.0 kDa
Excluded volume excluded_volume22782 ų
Envelope volume envelope_volume24707 ų
Hydration-shell volume shell_volume13914 ų
Envelope diameter envelope_diameter50.6
Shell Rg shell_rg20.78
Envelope Rg envelope_rg15.23
Shape Rg shape_rg15.01
Total Rg total_rg16.18
Total atoms total_atoms1266
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 dmax50.1
Rg (real space) rg_real16.25
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real5.5840e+06
I(0) uncertainty (real space) i0_real_error5.7820e+04
Rg (reciprocal space) rg_reciprocal16.27
I(0) (reciprocal space) i0_reciprocal5584000.0000
Solution quality estimate total_estimate0.6888
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.2
Skewness Skewness skewness0.081
Kurtosis Kurtosis kurtosis-0.460
Angular range angular_range— – 0.4850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha853100.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 0.998; Sysdev: 0.409; Positv: 1.000; Valcen: 0.982; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3h57a_
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_id3h57A00
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)