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1rsx

12-mer from site II calbindin D9K (DKNGDGEVSFEE) coordinating Cd(II)

Method: SOLUTION NMR Dmax: 22.9 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Vitamin D-dependent calcium-binding protein, intestinal

OrganismNot specified

UniProt P02632

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 57–68 Fragment：residues 57-68 (SWS P02632) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.6；288 K；Ionic strength (raw mmCIF value) aprox 0；Pressure ambient NMR sample composition：3mM Peptide and Cd(NO3)2. NaOH and HNO3 added for pH fixing to 6.6; 80% H2O, 20% D2O | 80% H2O, 20% D2O Resolution not provided

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.

Other PDB Difference from Current Entry 1RSX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CB1 THREE-DIMENSIONAL SOLUTION STRUCTURE OF CA2+-LOADED PORCINE CALBINDIN D9K DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY Deposited 1991-12-13 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–78（78 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1RSW 12-mer from site II calbindin D9K (DKNGDGEVSFEE) coordination Pb(II) Deposited 2003-12-10 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 57–68（12 aa） Fragment：residues 57-68
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.4；288 K；Ionic strength (raw mmCIF value) aprox 0；Pressure ambient
NMR sample composition 3mM Peptide and Pb(NO3)2. NaOH and HNO3 added for pH fixing to 5.4; 80% H2O, 20% D2O. | 80% H2O, 20% D2O
Resolution not provided

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S100G_PIG
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–12； UniProt 57–68

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 1rsx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1rsx
Deposition date deposition_date2003-12-10
Structure title title12-mer from site II calbindin D9K (DKNGDGEVSFEE) coordinating Cd(II)
Keywords keywordsEF-hand toxic metal ion transport model of ICaBP coordination toward cadmium, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier5.86 Å
Radius of gyration Rg (electron density) rg_electron5.77 Å
Forward intensity I(0) i03692450.00
Molecular weight molecular_weight13043.0 kDa
Excluded volume excluded_volume15287 ų
Envelope volume envelope_volume3386 ų
Hydration-shell volume shell_volume4369 ų
Envelope diameter envelope_diameter23.4 Å
Shell Rg shell_rg11.86 Å
Envelope Rg envelope_rg7.49 Å
Shape Rg shape_rg5.76 Å
Total Rg total_rg6.43 Å
Total atoms total_atoms1510
Residues n_residues120
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax22.9 Å
Rg (real space) rg_real5.92 Å
Rg uncertainty (real space) rg_real_error0.41 Å
I(0) (real space) i0_real3.6920e+06
I(0) uncertainty (real space) i0_real_error3.7750e+04
Rg (reciprocal space) rg_reciprocal5.92 Å
I(0) (reciprocal space) i0_reciprocal3692000.0000
Solution quality estimate total_estimate0.7465
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary22.4 Å
Skewness Skewness skewness0.688
Kurtosis Kurtosis kurtosis0.549
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha706.1000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.478; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.537; Smooth: 0.746
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)