5ntc

Crystal structure of mouse CARM1 in complex with inhibitor SA0678

Method: X-RAY DIFFRACTION Dmax: 127.7 Å Quality: EXCELLENT

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 130–497 Chain B; UniProt 130–497 Chain C; UniProt 130–497 Chain D; UniProt 130–497 Not recorded EDO 1,2-ETHANEDIOL × 13 PEG DI(HYDROXYETHYL)ETHER × 2 DXE 1,2-DIMETHOXYETHANE × 2 M2M 1-METHOXY-2-(2-METHOXYETHOXY)ETHANE × 1 B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 3 6L7 [(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-(2-azaniumylethyl)-[(3~{S})-3-azaniumyl-4-oxidanyl-4-oxidanylidene-butyl]azanium × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;297 K;BTP pH 7.5 100 mM, PEG 2000 MME 25 %, NaCl 50 mM Resolution 2.25 Å R-free 0.216

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
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

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 5ntc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5ntc
Deposition date deposition_date2017-04-27
Structure title titleCrystal structure of mouse CARM1 in complex with inhibitor SA0678
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_guinier39.75
Radius of gyration Rg (electron density) rg_electron39.39
Forward intensity I(0) i0351326000.00
Molecular weight molecular_weight158270.0 kDa
Excluded volume excluded_volume199940 ų
Envelope volume envelope_volume256370 ų
Hydration-shell volume shell_volume54411 ų
Envelope diameter envelope_diameter129.3
Shell Rg shell_rg45.28
Envelope Rg envelope_rg38.59
Shape Rg shape_rg39.36
Total Rg total_rg39.83
Total atoms total_atoms22146
Residues n_residues1364
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 dmax127.7
Rg (real space) rg_real39.71
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real3.5130e+08
I(0) uncertainty (real space) i0_real_error5.1760e+06
Rg (reciprocal space) rg_reciprocal39.74
I(0) (reciprocal space) i0_reciprocal351300000.0000
Solution quality estimate total_estimate0.9009
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.9
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.618
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha43670000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.883

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5ntcb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamilyc.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family familyc.66.1.6 — Arginine methyltransferase
Domain ID domain_idd5ntcd_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamilyc.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family familyc.66.1.6 — Arginine methyltransferase

CATH v4.4 (4 domains)

Domain ID domain_id5ntcA02
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_id5ntcB02
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_id5ntcC02
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_id5ntcD02
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)