5wp6

Cryo-EM structure of a human TRPM4 channel in complex with calcium and decavanadate

Method: ELECTRON MICROSCOPY Dmax: 169.8 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 DVT DECAVANADATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 5wp6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5wp6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5wp6
Deposition date deposition_date2017-08-03
Structure title titleCryo-EM structure of a human TRPM4 channel in complex with calcium and decavanadate
Keywords keywordsIon 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_guinier54.35
Radius of gyration Rg (electron density) rg_electron53.82
Forward intensity I(0) i02350850000.00
Molecular weight molecular_weight413470.0 kDa
Excluded volume excluded_volume519480 ų
Envelope volume envelope_volume857050 ų
Hydration-shell volume shell_volume128670 ų
Envelope diameter envelope_diameter173.2
Shell Rg shell_rg61.51
Envelope Rg envelope_rg51.48
Shape Rg shape_rg53.89
Total Rg total_rg53.79
Total atoms total_atoms29036
Residues n_residues3908
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 dmax169.8
Rg (real space) rg_real54.06
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real2.3510e+09
I(0) uncertainty (real space) i0_real_error4.1370e+07
Rg (reciprocal space) rg_reciprocal54.57
I(0) (reciprocal space) i0_reciprocal2353000000.0000
Solution quality estimate total_estimate0.8733
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.3
Skewness Skewness skewness0.120
Kurtosis Kurtosis kurtosis-0.436
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha338200000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.710

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5wp6b1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.14 — Gated ion channels
Superfamily Superfamily superfamilyf.14.1 — Voltage-gated ion channels
Family Family familyf.14.1.4 — TRPM-like (melastatin-like transient receptor potential) channels
Domain ID domain_idd5wp6b2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamilyd.211.1 — Ankyrin repeat
Family Family familyd.211.1.1 — Ankyrin repeat
Domain ID domain_idd5wp6b3
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.129 — MCP/YpsA-like
Superfamily Superfamily superfamilyc.129.1 — MCP/YpsA-like
Family Family familyc.129.1.3 — SMF/DprA-LOG (SLOG) domain from TPRM channels

8. Citations (1)

9. Files and Curves (10)