2v74

Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), in complex with S-adenosyl-homocysteine

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 147–490 Chain D; UniProt 147–490 Fragment:CATALYTIC DOMAIN, RESIDUES 147-490 SAH S-ADENOSYL-L-HOMOCYSTEINE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;1.6M DI-AMMONIUM HYDROGENPHOSPHATE, 100MM HEPES PH 7.5. Resolution 2.70 Å R-free 0.273
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 147–490 Chain H; UniProt 147–490 Fragment:CATALYTIC DOMAIN, RESIDUES 147-490 SAH S-ADENOSYL-L-HOMOCYSTEINE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;1.6M DI-AMMONIUM HYDROGENPHOSPHATE, 100MM HEPES PH 7.5. Resolution 2.70 Å R-free 0.273

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 B; PDBConstruct 3–346; UniProt 147–490 Author chain D; PDBConstruct 3–346; UniProt 147–490 Author chain F; PDBConstruct 3–346; UniProt 147–490 Author chain H; PDBConstruct 3–346; UniProt 147–490

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 2v74

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2v74
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2v74
Deposition date deposition_date2007-07-26
Structure title titleCrystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), in complex with S-adenosyl-homocysteine
Keywords keywords;ARGININE METHYLTRANSFERASE, S-ADENOSYL-L-METHIONINE, TRANSCRIPTION REGULATION, ALTERNATIVE SPLICING, HISTONE MODIFICATION, CO- ACTIVATOR, METHYLTRANSFERASE, CHROMATIN REGULATOR, NUCLEUS, CYTOPLASM, TRANSFERASE, TRANSCRIPTION ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.81
Radius of gyration Rg (electron density) rg_electron39.52
Forward intensity I(0) i0316748000.00
Molecular weight molecular_weight149720.0 kDa
Excluded volume excluded_volume188760 ų
Envelope volume envelope_volume239560 ų
Hydration-shell volume shell_volume51111 ų
Envelope diameter envelope_diameter132.2
Shell Rg shell_rg44.55
Envelope Rg envelope_rg38.71
Shape Rg shape_rg39.48
Total Rg total_rg39.94
Total atoms total_atoms10571
Residues n_residues1326
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_real39.80
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real3.1670e+08
I(0) uncertainty (real space) i0_real_error5.4490e+06
Rg (reciprocal space) rg_reciprocal39.81
I(0) (reciprocal space) i0_reciprocal316800000.0000
Solution quality estimate total_estimate0.8986
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.613
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34870000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.870

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2v74b_
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_idd2v74d_
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_idd2v74f_
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_idd2v74h_
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 (8 domains)

Domain ID domain_id2v74B01
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_id2v74B02
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_id2v74D01
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_id2v74D02
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_id2v74F01
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_id2v74F02
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_id2v74H01
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_id2v74H02
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)