8w2l

TRPM7 structure in complex with anticancer agent CCT128930 in closed state

Method: ELECTRON MICROSCOPY Dmax: 166.1 Å Quality: GOOD

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

Green fluorescent protein,Transient receptor potential cation channel subfamily M member 7

Mus musculus

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–238 Chain B; UniProt 2–238 Chain C; UniProt 2–238 Chain D; UniProt 2–238 Fragment:residues 3-1280 of the TRPM7 channel POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 52 CLR CHOLESTEROL × 4 M05 4-(4-chlorobenzyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-aminium × 4 DU0 2-[2-[(1~{S},2~{S},4~{S},5'~{R},6~{R},7~{S},8~{R},9~{S},12~{S},13~{R},16~{S})-5',7,9,13-tetramethylspiro[5-oxapentacyclo[10.8.0.0^{2,9}.0^{4,8}.0^{13,18}]icos-18-ene-6,2'-oxane]-16-yl]oxyethyl]propane-1,3-diol × 4 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.45 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–247; UniProt 2–238 Author chain B; PDBConstruct 11–247; UniProt 2–238 Author chain C; PDBConstruct 11–247; UniProt 2–238 Author chain D; PDBConstruct 11–247; UniProt 2–238

Green fluorescent protein,Transient receptor potential cation channel subfamily M member 7

Mus musculus

UniProt Q923J1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 3–1280 Chain B; UniProt 3–1280 Chain C; UniProt 3–1280 Chain D; UniProt 3–1280 Fragment:residues 3-1280 of the TRPM7 channel POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 52 CLR CHOLESTEROL × 4 M05 4-(4-chlorobenzyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-aminium × 4 DU0 2-[2-[(1~{S},2~{S},4~{S},5'~{R},6~{R},7~{S},8~{R},9~{S},12~{S},13~{R},16~{S})-5',7,9,13-tetramethylspiro[5-oxapentacyclo[10.8.0.0^{2,9}.0^{4,8}.0^{13,18}]icos-18-ene-6,2'-oxane]-16-yl]oxyethyl]propane-1,3-diol × 4 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.45 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRPM7_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 257–1534; UniProt 3–1280 Author chain B; PDBConstruct 257–1534; UniProt 3–1280 Author chain C; PDBConstruct 257–1534; UniProt 3–1280 Author chain D; PDBConstruct 257–1534; UniProt 3–1280

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 8w2l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8w2l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8w2l
Deposition date deposition_date2024-02-20
Structure title titleTRPM7 structure in complex with anticancer agent CCT128930 in closed state
Keywords keywordstransient receptor potential M family member 7, TRP, channel, TRPM7, TRP channels, membrane protein, CCT128930; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.16
Radius of gyration Rg (electron density) rg_electron52.88
Forward intensity I(0) i02843330000.00
Molecular weight molecular_weight506590.0 kDa
Excluded volume excluded_volume658200 ų
Envelope volume envelope_volume938080 ų
Hydration-shell volume shell_volume139840 ų
Envelope diameter envelope_diameter165.8
Shell Rg shell_rg63.15
Envelope Rg envelope_rg50.87
Shape Rg shape_rg52.88
Total Rg total_rg53.20
Total atoms total_atoms35633
Residues n_residues4056
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 dmax166.1
Rg (real space) rg_real52.82
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real2.8430e+09
I(0) uncertainty (real space) i0_real_error5.8460e+07
Rg (reciprocal space) rg_reciprocal53.43
I(0) (reciprocal space) i0_reciprocal2846000000.0000
Solution quality estimate total_estimate0.8739
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.0
Skewness Skewness skewness0.041
Kurtosis Kurtosis kurtosis-0.456
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha424100000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.932; Smooth: 0.852

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)