9i1t

CARM1 in complex with arg-MMA analog

Method: X-RAY DIFFRACTION Dmax: 130.2 Å Quality: GOOD

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

Histone-arginine methyltransferase CARM1

Mus musculus

UniProt Q9WVG6

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 130–487 Chain B; UniProt 130–487 Not recorded A1IZ2 (phenylmethyl) (2S)-5-[[N-[3-[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]propyl]carbamimidoyl]amino]-2-(phenylmethoxycarbonylamino)pentanoate × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;9% PEG3350, 100mM Tris HCl pH7.5, 0.2M ammonium sulfate Resolution 2.39 Å R-free 0.238
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 130–487 Chain D; UniProt 130–487 Not recorded A1IZ2 (phenylmethyl) (2S)-5-[[N-[3-[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]propyl]carbamimidoyl]amino]-2-(phenylmethoxycarbonylamino)pentanoate × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;9% PEG3350, 100mM Tris HCl pH7.5, 0.2M ammonium sulfate Resolution 2.39 Å R-free 0.238

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.

42 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CARM1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–361; UniProt 130–487 Author chain B; PDBConstruct 4–361; UniProt 130–487 Author chain C; PDBConstruct 4–361; UniProt 130–487 Author chain D; PDBConstruct 4–361; UniProt 130–487

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 9i1t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9i1t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9i1t
Deposition date deposition_date2025-01-16
最后修订 last_revision2026-01-28
Structure title titleCARM1 in complex with arg-MMA analog
Keywords keywordsprotein arginine N-methyltransferase, PRMT, CARM1, transition state mimics, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.06
Radius of gyration Rg (electron density) rg_electron39.70
Forward intensity I(0) i0349672000.00
Molecular weight molecular_weight158700.0 kDa
Excluded volume excluded_volume200550 ų
Envelope volume envelope_volume251340 ų
Hydration-shell volume shell_volume52909 ų
Envelope diameter envelope_diameter133.1
Shell Rg shell_rg45.21
Envelope Rg envelope_rg39.01
Shape Rg shape_rg39.80
Total Rg total_rg39.66
Total atoms total_atoms22180
Residues n_residues1372
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 dmax130.2
Rg (real space) rg_real40.05
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real3.4970e+08
I(0) uncertainty (real space) i0_real_error6.5500e+06
Rg (reciprocal space) rg_reciprocal40.06
I(0) (reciprocal space) i0_reciprocal349700000.0000
Solution quality estimate total_estimate0.8981
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.7
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.646
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha38800000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.910

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)