5lgs

Crystal structure of mouse CARM1 in complex with ligand P2C3u

Method: X-RAY DIFFRACTION Dmax: 129.4 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 130–487 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 DXE 1,2-DIMETHOXYETHANE × 3 PEG DI(HYDROXYETHYL)ETHER × 1 PG4 TETRAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 3 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 8;293 K;Tris-HCl pH 8.5 100 mM PEG 3350 20 % A.S. 200 mM Resolution 2.10 Å R-free 0.215

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 456–464 Chain F; UniProt 456–464 Chain G; UniProt 456–464 Chain H; UniProt 456–464 Not recorded Histone-arginine methyltransferase CARM1 × 4 (Q9WVG6) SO4 SULFATE ION × 1 DXE 1,2-DIMETHOXYETHANE × 3 PEG DI(HYDROXYETHYL)ETHER × 1 PG4 TETRAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 3 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 8;293 K;Tris-HCl pH 8.5 100 mM PEG 3350 20 % A.S. 200 mM Resolution 2.10 Å R-free 0.215

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 1–9; UniProt 456–464 Author chain F; PDBConstruct 1–9; UniProt 456–464 Author chain G; PDBConstruct 1–9; UniProt 456–464 Author chain H; PDBConstruct 1–9; UniProt 456–464

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 5lgs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5lgs
Deposition date deposition_date2016-07-08
Structure title titleCrystal structure of mouse CARM1 in complex with ligand P2C3u
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_guinier39.83
Radius of gyration Rg (electron density) rg_electron39.51
Forward intensity I(0) i0366210000.00
Molecular weight molecular_weight161530.0 kDa
Excluded volume excluded_volume203800 ų
Envelope volume envelope_volume252440 ų
Hydration-shell volume shell_volume53222 ų
Envelope diameter envelope_diameter130.8
Shell Rg shell_rg45.37
Envelope Rg envelope_rg38.92
Shape Rg shape_rg39.47
Total Rg total_rg39.98
Total atoms total_atoms22590
Residues n_residues1406
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 dmax129.4
Rg (real space) rg_real39.83
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real3.6620e+08
I(0) uncertainty (real space) i0_real_error5.3660e+06
Rg (reciprocal space) rg_reciprocal39.84
I(0) (reciprocal space) i0_reciprocal366200000.0000
Solution quality estimate total_estimate0.8988
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.3
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.649
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha60350000.0000
Real-space data points n_real_points41
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: 0.979; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id5lgsA01
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_id5lgsA02
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_id5lgsB01
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_id5lgsB02
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_id5lgsC01
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_id5lgsC02
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_id5lgsD01
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_id5lgsD02
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)