5lgr

Crystal structure of mouse CARM1 in complex with ligand P1C3u

Method: X-RAY DIFFRACTION Dmax: 129.2 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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 130–487 Chain B; UniProt 130–487 Chain C; UniProt 130–487 Chain D; UniProt 130–487 Not recorded Polyadenylate-binding protein 1 × 4 (P11940) SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 6 DXE 1,2-DIMETHOXYETHANE × 1 PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE × 1 PEG DI(HYDROXYETHYL)ETHER × 1 QVR (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[(~{E})-prop-1-enyl]oxolane-3,4-diol × 4 LPD L-PROLINAMIDE × 4 ACE ACETYL GROUP × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;Tris-HCl pH 8.5 100 mM PEG 3350 14 % Ammonium Sulfate 200 mM Resolution 2.00 Å R-free 0.234

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 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CARM1_MOUSE
Isoform Q9WVG6-2
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

Polyadenylate-binding protein 1

OrganismNot specified

UniProt P11940

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 447–458 Chain F; UniProt 447–458 Chain G; UniProt 447–458 Chain H; UniProt 447–458 Not recorded Histone-arginine methyltransferase CARM1 × 4 (Q9WVG6) SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 6 DXE 1,2-DIMETHOXYETHANE × 1 PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE × 1 PEG DI(HYDROXYETHYL)ETHER × 1 QVR (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[(~{E})-prop-1-enyl]oxolane-3,4-diol × 4 LPD L-PROLINAMIDE × 4 ACE ACETYL GROUP × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;Tris-HCl pH 8.5 100 mM PEG 3350 14 % Ammonium Sulfate 200 mM Resolution 2.00 Å R-free 0.234

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.

27 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PABP1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–12; UniProt 447–458 Author chain F; PDBConstruct 1–12; UniProt 447–458 Author chain G; PDBConstruct 1–12; UniProt 447–458 Author chain H; PDBConstruct 1–12; UniProt 447–458

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 5lgr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5lgr
Deposition date deposition_date2016-07-08
Structure title titleCrystal structure of mouse CARM1 in complex with ligand P1C3u
Keywords keywords;PROTEIN ARGININE METHYLTRANSFERASE, CATALYTIC DOMAIN, CHROMATIN REGULATOR, MRNA PROCESSING, MRNA SPLICING, NUCLEUS, S-ADENOSYL-L-METHIONINE, TRANSCRIPTION, TRANSCRIPTION REGULATION, TRANSFERASE ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.74
Radius of gyration Rg (electron density) rg_electron39.45
Forward intensity I(0) i0375438000.00
Molecular weight molecular_weight163260.0 kDa
Excluded volume excluded_volume205880 ų
Envelope volume envelope_volume252930 ų
Hydration-shell volume shell_volume53222 ų
Envelope diameter envelope_diameter132.8
Shell Rg shell_rg45.41
Envelope Rg envelope_rg39.00
Shape Rg shape_rg39.42
Total Rg total_rg39.90
Total atoms total_atoms22832
Residues n_residues1417
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 dmax129.2
Rg (real space) rg_real39.75
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real3.7540e+08
I(0) uncertainty (real space) i0_real_error6.7700e+06
Rg (reciprocal space) rg_reciprocal39.75
I(0) (reciprocal space) i0_reciprocal375400000.0000
Solution quality estimate total_estimate0.8976
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.2
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.647
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha73270000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.902

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id5lgrA01
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_id5lgrA02
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_id5lgrB01
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_id5lgrB02
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_id5lgrC01
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_id5lgrC02
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_id5lgrD01
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_id5lgrD02
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)