9kdf

CryoEM structure of Calcineurin-fusion Human endothelin receptor type-B in complex with RES-701-3

Method: ELECTRON MICROSCOPY Dmax: 128.4 Å Quality: GOOD

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

Peptidyl-prolyl cis-trans isomerase FKBP1B

Homo sapiens

UniProt P68106

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 2–108 Not recorded Calcineurin-fusion endothelin receptor type-B × 1 RES-701-3 × 1 CA CALCIUM ION × 4 FE FE (III) ION × 1 ZN ZINC ION × 1 FK5 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

117 other PDB entries and 119 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FKB1B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 4–110; UniProt 2–108

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 9kdf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9kdf
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9kdf
Deposition date deposition_date2024-11-03
Structure title titleCryoEM structure of Calcineurin-fusion Human endothelin receptor type-B in complex with RES-701-3
Keywords keywordsGPCR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.17
Radius of gyration Rg (electron density) rg_electron38.17
Forward intensity I(0) i0153505000.00
Molecular weight molecular_weight105270.0 kDa
Excluded volume excluded_volume133700 ų
Envelope volume envelope_volume175970 ų
Hydration-shell volume shell_volume39604 ų
Envelope diameter envelope_diameter137.1
Shell Rg shell_rg42.33
Envelope Rg envelope_rg38.15
Shape Rg shape_rg38.19
Total Rg total_rg38.35
Total atoms total_atoms7399
Residues n_residues917
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 dmax128.4
Rg (real space) rg_real38.44
Rg uncertainty (real space) rg_real_error1.57
I(0) (real space) i0_real1.5350e+08
I(0) uncertainty (real space) i0_real_error3.1470e+06
Rg (reciprocal space) rg_reciprocal38.28
I(0) (reciprocal space) i0_reciprocal153500000.0000
Solution quality estimate total_estimate0.7925
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.3
Skewness Skewness skewness0.406
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29210000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.823; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.831; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)