1ig5

BOVINE CALBINDIN D9K BINDING MG2+

Method: X-RAY DIFFRACTION Dmax: 39.2 Å Quality: GOOD

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

VITAMIN D-DEPENDENT CALCIUM-BINDING PROTEIN, INTESTINAL

Bos taurus

UniProt P02633

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 4–78 Not recorded MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.4;298 K;3M ammonium sulphate, 100 mM magnesium chloride, pH 6.4, EVAPORATION, temperature 298K Resolution 1.50 Å R-free 0.285

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.

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

View Construct and Data Evidence
UniProt name S100G_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–75; UniProt 4–78

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 1ig5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ig5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1ig5
Deposition date deposition_date2001-04-17
Structure title titleBOVINE CALBINDIN D9K BINDING MG2+
Keywords keywordsCALCIUM-BINDING PROTEIN, EF-HAND, MAGNESIUM BINDING, 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_guinier13.06
Radius of gyration Rg (electron density) rg_electron11.39
Forward intensity I(0) i01484740.00
Molecular weight molecular_weight8460.0 kDa
Excluded volume excluded_volume10743 ų
Envelope volume envelope_volume11724 ų
Hydration-shell volume shell_volume8953 ų
Envelope diameter envelope_diameter36.0
Shell Rg shell_rg16.76
Envelope Rg envelope_rg11.62
Shape Rg shape_rg11.36
Total Rg total_rg12.90
Total atoms total_atoms597
Residues n_residues75
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 dmax39.2
Rg (real space) rg_real12.95
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real1.4850e+06
I(0) uncertainty (real space) i0_real_error1.5090e+04
Rg (reciprocal space) rg_reciprocal12.95
I(0) (reciprocal space) i0_reciprocal1485000.0000
Solution quality estimate total_estimate0.8966
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.9
Skewness Skewness skewness-0.028
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha168800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.974

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_idd1ig5a_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.1 — Calbindin D9K

CATH v4.4 (1 domains)

Domain ID domain_id1ig5A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (1)

9. Files and Curves (10)