7os4

Crystal structure of mouse CARM1 in complex with histone H3_13-31 K18

Method: X-RAY DIFFRACTION Dmax: 128.4 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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 130–497 Chain B; UniProt 130–497 Not recorded Histone H3.1 × 4 (P68433) QVR (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[(~{E})-prop-1-enyl]oxolane-3,4-diol × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;1.2M Sodium malonate 0.1M MES pH 5.5 0.2M NaCl Resolution 2.54 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 130–497 Chain D; UniProt 130–497 Not recorded Histone H3.1 × 4 (P68433) QVR (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[(~{E})-prop-1-enyl]oxolane-3,4-diol × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;1.2M Sodium malonate 0.1M MES pH 5.5 0.2M NaCl Resolution 2.54 Å R-free 0.255

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 4–371; UniProt 130–497 Author chain B; PDBConstruct 4–371; UniProt 130–497 Author chain C; PDBConstruct 4–371; UniProt 130–497 Author chain D; PDBConstruct 4–371; UniProt 130–497

Histone H3.1

OrganismNot specified

UniProt P68433

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 14–32 Chain F; UniProt 14–32 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone-arginine methyltransferase CARM1 × 4 (Q9WVG6) QVR (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[(~{E})-prop-1-enyl]oxolane-3,4-diol × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;1.2M Sodium malonate 0.1M MES pH 5.5 0.2M NaCl Resolution 2.54 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 14–32 Chain H; UniProt 14–32 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone-arginine methyltransferase CARM1 × 4 (Q9WVG6) QVR (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[(~{E})-prop-1-enyl]oxolane-3,4-diol × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;1.2M Sodium malonate 0.1M MES pH 5.5 0.2M NaCl Resolution 2.54 Å R-free 0.255

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 2–20; UniProt 14–32 Author chain F; PDBConstruct 2–20; UniProt 14–32 Author chain G; PDBConstruct 2–20; UniProt 14–32 Author chain H; PDBConstruct 2–20; UniProt 14–32

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 7os4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7os4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7os4
Deposition date deposition_date2021-06-07
Structure title titleCrystal structure of mouse CARM1 in complex with histone H3_13-31 K18
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_guinier39.57
Radius of gyration Rg (electron density) rg_electron39.22
Forward intensity I(0) i0383341000.00
Molecular weight molecular_weight164670.0 kDa
Excluded volume excluded_volume207610 ų
Envelope volume envelope_volume258390 ų
Hydration-shell volume shell_volume54690 ų
Envelope diameter envelope_diameter130.9
Shell Rg shell_rg45.22
Envelope Rg envelope_rg38.62
Shape Rg shape_rg39.18
Total Rg total_rg39.65
Total atoms total_atoms11624
Residues n_residues1445
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_real39.55
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real3.8330e+08
I(0) uncertainty (real space) i0_real_error6.4360e+06
Rg (reciprocal space) rg_reciprocal39.57
I(0) (reciprocal space) i0_reciprocal383300000.0000
Solution quality estimate total_estimate0.8298
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.9
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.641
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha57650000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id7os4A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id7os4A02
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology160 — Hnrnp arginine n-methyltransferase1
Homologous superfamily homologous superfamily11 — Hnrnp arginine n-methyltransferase1
Domain ID domain_id7os4B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id7os4B02
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology160 — Hnrnp arginine n-methyltransferase1
Homologous superfamily homologous superfamily11 — Hnrnp arginine n-methyltransferase1
Domain ID domain_id7os4C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id7os4C02
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology160 — Hnrnp arginine n-methyltransferase1
Homologous superfamily homologous superfamily11 — Hnrnp arginine n-methyltransferase1
Domain ID domain_id7os4D01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id7os4D02
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology160 — Hnrnp arginine n-methyltransferase1
Homologous superfamily homologous superfamily11 — Hnrnp arginine n-methyltransferase1

8. Citations (1)

9. Files and Curves (10)