2kuh

Halothane binds to druggable sites in calcium-calmodulin: Solution structure of halothane-CaM C-terminal domain

Method: SOLUTION NMR Dmax: 37.5 Å Quality: GOOD

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

Calmodulin

Homo sapiens

UniProt P62158

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 83–149 Fragment:C-TERMINAL DOMAIN EF-hands 3 and 4 CA CALCIUM ION × 2 HLT 2-BROMO-2-CHLORO-1,1,1-TRIFLUOROETHANE × 1 SOLUTION NMR NMR measurement conditions:pH 7.2;298 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient NMR sample composition:2 mM [U-99% 13C; U-99% 15N] CALCIUM ION, 20 mM CALCIUM ION, 20 mM N-{[2-({[1-(4-CARBOXYBUTANOYL)AMINO]-2-PHENYLETHYL}-HYDROXYPHOSPHINYL)OXY]ACETYL}-2-PHENYLETHYLAMINE, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:2 mM [U-99% 15N] CALCIUM ION, 20 mM CALCIUM ION, 20 mM N-{[2-({[1-(4-CARBOXYBUTANOYL)AMINO]-2-PHENYLETHYL}-HYDROXYPHOSPHINYL)OXY]ACETYL}-2-PHENYLETHYLAMINE, 95% H2O/5% D2O | 95% H2O/5% 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.

105 other PDB entries and 176 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–67; UniProt 83–149

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 2kuh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2kuh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2kuh
Deposition date deposition_date2010-02-17
Structure title titleHalothane binds to druggable sites in calcium-calmodulin: Solution structure of halothane-CaM C-terminal domain
Keywords keywords;CALMODULIN, CALCIUM BINDING, VOLATILE ANESTHETIC, HALOTHANE, Cytoskeleton, Isopeptide bond, Methylation, Phosphoprotein, METAL BINDING PROTEIN ;; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.73
Radius of gyration Rg (electron density) rg_electron11.28
Forward intensity I(0) i029172300.00
Molecular weight molecular_weight39975.0 kDa
Excluded volume excluded_volume48116 ų
Envelope volume envelope_volume12724 ų
Hydration-shell volume shell_volume9284 ų
Envelope diameter envelope_diameter39.7
Shell Rg shell_rg17.36
Envelope Rg envelope_rg12.25
Shape Rg shape_rg11.31
Total Rg total_rg11.59
Total atoms total_atoms5265
Residues n_residues335
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 dmax37.5
Rg (real space) rg_real11.65
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real2.9170e+07
I(0) uncertainty (real space) i0_real_error3.0300e+05
Rg (reciprocal space) rg_reciprocal11.65
I(0) (reciprocal space) i0_reciprocal29170000.0000
Solution quality estimate total_estimate0.8861
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.2
Skewness Skewness skewness0.039
Kurtosis Kurtosis kurtosis-0.356
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha78310.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.956

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2kuha_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.5 — Calmodulin-like

8. Citations (1)

9. Files and Curves (10)