1nz4

The horse heart myoglobin variant K45E/K63E complexed with Cadmium

Method: X-RAY DIFFRACTION Dmax: 49.9 Å Quality: EXCELLENT

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

Myoglobin

Equus caballus

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 A; UniProt 1–153 Mutation:K45E, K63E CD CADMIUM ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;298 K;ammonium sulfate, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.80 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.

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 A; 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 1nz4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1nz4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1nz4
Deposition date deposition_date2003-02-15
Structure title titleThe horse heart myoglobin variant K45E/K63E complexed with Cadmium
Keywords keywordscadmium Cd2+ horse heart myoglobin engineered metal binding site, 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_guinier16.64
Radius of gyration Rg (electron density) rg_electron15.18
Forward intensity I(0) i05874740.00
Molecular weight molecular_weight17791.0 kDa
Excluded volume excluded_volume22271 ų
Envelope volume envelope_volume24657 ų
Hydration-shell volume shell_volume13866 ų
Envelope diameter envelope_diameter48.6
Shell Rg shell_rg20.80
Envelope Rg envelope_rg15.28
Shape Rg shape_rg15.14
Total Rg total_rg16.33
Total atoms total_atoms1244
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 dmax49.9
Rg (real space) rg_real16.50
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real5.8750e+06
I(0) uncertainty (real space) i0_real_error6.6640e+04
Rg (reciprocal space) rg_reciprocal16.52
I(0) (reciprocal space) i0_reciprocal5875000.0000
Solution quality estimate total_estimate0.9070
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.6
Skewness Skewness skewness0.065
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha800100.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.981

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_idd1nz4a_
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_id1nz4A00
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)