9zmd

Equine Serum Albumin with Copper(II)

Method: X-RAY DIFFRACTION Dmax: 87.6 Å Quality: EXCELLENT

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

Serum albumin

OrganismNot specified

UniProt P35747

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 25–607 Not recorded CU COPPER (II) ION × 6 SO4 SULFATE ION × 7 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;291.15 K;0.2 M lithium sulfate, 0.1 M Tris-HCl, pH 7.4, 2.2 M ammonium sulfate, 5 mM copper(II) chloride mixed 1:1 with 36 mg/mL protein, 10 mM Tris-HCl, 150 mM sodium chloride Resolution 2.65 Å R-free 0.251

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.

23 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ALBU_HORSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–583; UniProt 25–607

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 9zmd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zmd
Deposition date deposition_date2025-12-10
最后修订 last_revision2025-12-24
Structure title titleEquine Serum Albumin with Copper(II)
Keywords keywords;TRANSPORT PROTEIN, COPPER, METAL BINDING, Structural Genomics, PSI-Biology, New York Structural Genomics Research Consortium, NYSGRC, METAL BINDING PROTEIN ;; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.56
Radius of gyration Rg (electron density) rg_electron26.56
Forward intensity I(0) i076807700.00
Molecular weight molecular_weight66750.0 kDa
Excluded volume excluded_volume82710 ų
Envelope volume envelope_volume102000 ų
Hydration-shell volume shell_volume32349 ų
Envelope diameter envelope_diameter92.9
Shell Rg shell_rg33.54
Envelope Rg envelope_rg26.56
Shape Rg shape_rg26.53
Total Rg total_rg27.36
Total atoms total_atoms4646
Residues n_residues583
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 dmax87.6
Rg (real space) rg_real27.46
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real7.6810e+07
I(0) uncertainty (real space) i0_real_error1.0360e+06
Rg (reciprocal space) rg_reciprocal27.49
I(0) (reciprocal space) i0_reciprocal76810000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.2
Skewness Skewness skewness0.227
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11040000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)