1a75

WHITING PARVALBUMIN

Method: X-RAY DIFFRACTION Dmax: 69.0 Å Quality: GOOD

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

PARVALBUMIN

OrganismNot specified

UniProt P02621

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 1–108 Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;SITTING DROP. RESERVOIR: 1 ML 2.1M NAH2PO4/NA2HPO4 (PH 6.0) 0.7M (NH4)2SO4, 0.02%(W/V) NAN3 DROP: 10 MICROL. PROTEIN SOLUTION (15MG/ML) +10 MICROL. RESERVOIR SOLUTION., vapor diffusion - sitting drop Resolution 1.90 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–108 Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;SITTING DROP. RESERVOIR: 1 ML 2.1M NAH2PO4/NA2HPO4 (PH 6.0) 0.7M (NH4)2SO4, 0.02%(W/V) NAN3 DROP: 10 MICROL. PROTEIN SOLUTION (15MG/ML) +10 MICROL. RESERVOIR SOLUTION., vapor diffusion - sitting drop Resolution 1.90 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name PRVB_MERMR
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–108; UniProt 1–108 Author chain B; PDBConstruct 2–109; UniProt 1–108

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 1a75

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a75
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a75
Deposition date deposition_date1998-03-19
Structure title titleWHITING PARVALBUMIN
Keywords keywordsCALCIUM BINDING PROTEIN, MUSCLE PROTEIN; CALCIUM BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.08
Radius of gyration Rg (electron density) rg_electron19.23
Forward intensity I(0) i08855920.00
Molecular weight molecular_weight22464.0 kDa
Excluded volume excluded_volume28258 ų
Envelope volume envelope_volume32670 ų
Hydration-shell volume shell_volume15209 ų
Envelope diameter envelope_diameter69.0
Shell Rg shell_rg23.94
Envelope Rg envelope_rg19.22
Shape Rg shape_rg19.20
Total Rg total_rg20.05
Total atoms total_atoms1575
Residues n_residues214
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 dmax69.0
Rg (real space) rg_real20.15
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real8.8560e+06
I(0) uncertainty (real space) i0_real_error1.2970e+05
Rg (reciprocal space) rg_reciprocal20.13
I(0) (reciprocal space) i0_reciprocal8856000.0000
Solution quality estimate total_estimate0.8451
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.7
Skewness Skewness skewness0.419
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1629000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.686; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.934; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1a75a_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.4 — Parvalbumin
Domain ID domain_idd1a75b_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.4 — Parvalbumin

CATH v4.4 (2 domains)

Domain ID domain_id1a75A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id1a75B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (5)

9. Files and Curves (10)