30kz

Human trpm4 in complex with PBA at 8 degrees Celsius

Method: ELECTRON MICROSCOPY Dmax: 171.3 Å Quality: GOOD

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

Transient receptor potential cation channel subfamily M member 4

Homo sapiens

UniProt Q8TD43

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1214 Chain B; UniProt 1–1214 Chain C; UniProt 1–1214 Chain D; UniProt 1–1214 Not recorded 4-methyl-2-[2-(3-prop-2-ynoxyphenoxy)ethanoylamino]benzoic acid × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.40 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.

37 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRPM4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1214; UniProt 1–1214 Author chain B; PDBConstruct 1–1214; UniProt 1–1214 Author chain C; PDBConstruct 1–1214; UniProt 1–1214 Author chain D; PDBConstruct 1–1214; UniProt 1–1214

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 30kz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 30kz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id30kz
Deposition date deposition_date2026-05-01
Structure title titleHuman trpm4 in complex with PBA at 8 degrees Celsius
Keywords keywordsTRP channel, ion channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.24
Radius of gyration Rg (electron density) rg_electron54.55
Forward intensity I(0) i02585380000.00
Molecular weight molecular_weight444270.0 kDa
Excluded volume excluded_volume563410 ų
Envelope volume envelope_volume867030 ų
Hydration-shell volume shell_volume129660 ų
Envelope diameter envelope_diameter170.7
Shell Rg shell_rg61.54
Envelope Rg envelope_rg51.88
Shape Rg shape_rg54.50
Total Rg total_rg54.92
Total atoms total_atoms62960
Residues n_residues3924
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 dmax171.3
Rg (real space) rg_real54.92
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real2.5850e+09
I(0) uncertainty (real space) i0_real_error4.9600e+07
Rg (reciprocal space) rg_reciprocal55.49
I(0) (reciprocal space) i0_reciprocal2588000000.0000
Solution quality estimate total_estimate0.8212
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary73.4
Skewness Skewness skewness0.084
Kurtosis Kurtosis kurtosis-0.479
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha277200000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)