5dxa

Crystal structure of CARM1, sinefungin, and methylated PABP1 peptide (R460)

Method: X-RAY DIFFRACTION Dmax: 128.2 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone-arginine methyltransferase CARM1

Homo sapiens

UniProt Q86X55

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 134–479 Chain B; UniProt 134–479 Fragment:catalytic domain (UNP residues 134-479) methylated PABP1 peptide × 2 (P11940) SFG SINEFUNGIN × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;291 K;0.2 M Ammonium Sulfate, 0.1 M Tris pH 8.5, 18% w/v PEG 3350 Resolution 2.07 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 134–479 Chain D; UniProt 134–479 Fragment:catalytic domain (UNP residues 134-479) methylated PABP1 peptide × 1 (P11940) SFG SINEFUNGIN × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;291 K;0.2 M Ammonium Sulfate, 0.1 M Tris pH 8.5, 18% w/v PEG 3350 Resolution 2.07 Å R-free 0.244

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.

32 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CARM1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–349; UniProt 134–479 Author chain B; PDBConstruct 4–349; UniProt 134–479 Author chain C; PDBConstruct 4–349; UniProt 134–479 Author chain D; PDBConstruct 4–349; UniProt 134–479

methylated PABP1 peptide

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 449–466 Chain G; UniProt 449–466 Fragment:UNP residues 449-466 Mutation:Nterminal biotin and aminohexanoic acid, methylated R460, asymmetrically dimethylated R455 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone-arginine methyltransferase CARM1 × 2 (Q86X55) SFG SINEFUNGIN × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;291 K;0.2 M Ammonium Sulfate, 0.1 M Tris pH 8.5, 18% w/v PEG 3350 Resolution 2.07 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 449–466 Fragment:UNP residues 449-466 Mutation:Nterminal biotin and aminohexanoic acid, methylated R460, asymmetrically dimethylated R455 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone-arginine methyltransferase CARM1 × 2 (Q86X55) SFG SINEFUNGIN × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;291 K;0.2 M Ammonium Sulfate, 0.1 M Tris pH 8.5, 18% w/v PEG 3350 Resolution 2.07 Å R-free 0.244

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 57 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 F; PDBConstruct 1–18; UniProt 449–466 Author chain G; PDBConstruct 1–18; UniProt 449–466 Author chain I; PDBConstruct 1–18; UniProt 449–466

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 5dxa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5dxa
Deposition date deposition_date2015-09-23
Structure title titleCrystal structure of CARM1, sinefungin, and methylated PABP1 peptide (R460)
Keywords keywordsprotein-substrate ternary complex, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.73
Radius of gyration Rg (electron density) rg_electron39.42
Forward intensity I(0) i0360795000.00
Molecular weight molecular_weight160130.0 kDa
Excluded volume excluded_volume201960 ų
Envelope volume envelope_volume249470 ų
Hydration-shell volume shell_volume52887 ų
Envelope diameter envelope_diameter130.6
Shell Rg shell_rg45.24
Envelope Rg envelope_rg38.76
Shape Rg shape_rg39.38
Total Rg total_rg39.87
Total atoms total_atoms11304
Residues n_residues1390
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 dmax128.2
Rg (real space) rg_real39.73
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real3.6080e+08
I(0) uncertainty (real space) i0_real_error6.3290e+06
Rg (reciprocal space) rg_reciprocal39.74
I(0) (reciprocal space) i0_reciprocal360800000.0000
Solution quality estimate total_estimate0.8990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.9
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.643
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51220000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id5dxaA01
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_id5dxaA02
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_id5dxaB01
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_id5dxaB02
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_id5dxaC01
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_id5dxaC02
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_id5dxaD01
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_id5dxaD02
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)