5va6

CRYSTAL STRUCTURE OF ATXR5 IN COMPLEX WITH HISTONE H3.1 MONO-METHYLATED ON R26

Method: X-RAY DIFFRACTION Dmax: 81.5 Å Quality: GOOD

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

Probable Histone-lysine N-methyltransferase ATXR5

Ricinus communis

UniProt B9RU15

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 146–374 Fragment:residues 146-374 Histone H3.1 × 1 (P68431) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;50% polypropylene glycol 400, 5% DMSO, 0.1 M HEPES-NaOH (pH 6.0) Resolution 2.40 Å R-free 0.297
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 146–374 Fragment:residues 146-374 Histone H3.1 × 1 (P68431) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;50% polypropylene glycol 400, 5% DMSO, 0.1 M HEPES-NaOH (pH 6.0) Resolution 2.40 Å R-free 0.297

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.

4 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATXR5_RICCO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–229; UniProt 146–374 Author chain B; PDBConstruct 1–229; UniProt 146–374

Histone H3.1

OrganismNot specified

UniProt P68431

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 20–37 Fragment:residues 20-37 Non-standard monomer:Yes (specific site not provided by mmCIF) Probable Histone-lysine N-methyltransferase ATXR5 × 1 (B9RU15) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;50% polypropylene glycol 400, 5% DMSO, 0.1 M HEPES-NaOH (pH 6.0) Resolution 2.40 Å R-free 0.297
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 20–37 Fragment:residues 20-37 Non-standard monomer:Yes (specific site not provided by mmCIF) Probable Histone-lysine N-methyltransferase ATXR5 × 1 (B9RU15) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;50% polypropylene glycol 400, 5% DMSO, 0.1 M HEPES-NaOH (pH 6.0) Resolution 2.40 Å R-free 0.297

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.

402 other PDB entries and 474 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–18; UniProt 20–37 Author chain D; PDBConstruct 1–18; UniProt 20–37

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 5va6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5va6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5va6
Deposition date deposition_date2017-03-24
Structure title titleCRYSTAL STRUCTURE OF ATXR5 IN COMPLEX WITH HISTONE H3.1 MONO-METHYLATED ON R26
Keywords keywordsnucleosome, TRANSFERASE-DNA BINDING PROTEIN complex; TRANSFERASE/DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.96
Radius of gyration Rg (electron density) rg_electron26.18
Forward intensity I(0) i047430200.00
Molecular weight molecular_weight50845.0 kDa
Excluded volume excluded_volume62529 ų
Envelope volume envelope_volume78529 ų
Hydration-shell volume shell_volume25167 ų
Envelope diameter envelope_diameter85.8
Shell Rg shell_rg33.10
Envelope Rg envelope_rg25.99
Shape Rg shape_rg26.19
Total Rg total_rg26.90
Total atoms total_atoms3554
Residues n_residues459
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 dmax81.5
Rg (real space) rg_real27.00
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real4.7430e+07
I(0) uncertainty (real space) i0_real_error7.2720e+05
Rg (reciprocal space) rg_reciprocal26.99
I(0) (reciprocal space) i0_reciprocal47430000.0000
Solution quality estimate total_estimate0.8946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.695
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7677000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.816

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5va6A00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology270 — Beta-clip-like
Homologous superfamily homologous superfamily10 — SET domain
Domain ID domain_id5va6B00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology270 — Beta-clip-like
Homologous superfamily homologous superfamily10 — SET domain

8. Citations (1)

9. Files and Curves (10)