2igq

Human euchromatic histone methyltransferase 1

Method: X-RAY DIFFRACTION Dmax: 87.6 Å Quality: GOOD

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

euchromatic histone methyltransferase 1

Homo sapiens

UniProt Q9H9B1

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 951–1235 Chain B; UniProt 951–1235 Fragment:C-terminal domain, residues 951-1235 ZN ZINC ION × 8 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;300 K;20% PEG 4K, 10% Isoproponol, 0.1M Hepes 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 300K Resolution 2.00 Å R-free 0.237

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.

21 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EHMT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–285; UniProt 951–1235 Author chain B; PDBConstruct 1–285; UniProt 951–1235

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 2igq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2igq
Deposition date deposition_date2006-09-23
Structure title titleHuman euchromatic histone methyltransferase 1
Keywords keywordseuchromatic histone methyltransferase 1, Structural Genomics, Structural Genomics Consortium, SGC, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.05
Radius of gyration Rg (electron density) rg_electron25.07
Forward intensity I(0) i067072100.00
Molecular weight molecular_weight59616.0 kDa
Excluded volume excluded_volume72560 ų
Envelope volume envelope_volume89778 ų
Hydration-shell volume shell_volume29883 ų
Envelope diameter envelope_diameter89.3
Shell Rg shell_rg32.50
Envelope Rg envelope_rg25.03
Shape Rg shape_rg25.07
Total Rg total_rg25.81
Total atoms total_atoms4136
Residues n_residues505
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 dmax87.6
Rg (real space) rg_real26.03
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real6.7070e+07
I(0) uncertainty (real space) i0_real_error9.9140e+05
Rg (reciprocal space) rg_reciprocal26.04
I(0) (reciprocal space) i0_reciprocal67070000.0000
Solution quality estimate total_estimate0.8794
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.6
Skewness Skewness skewness0.364
Kurtosis Kurtosis kurtosis-0.198
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6062000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.816; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2igqa_
Class classb — All beta proteins
Fold Fold foldb.85 — beta-clip
Superfamily Superfamily superfamilyb.85.7 — SET domain
Family Family familyb.85.7.0 — automated matches
Domain ID domain_idd2igqb_
Class classb — All beta proteins
Fold Fold foldb.85 — beta-clip
Superfamily Superfamily superfamilyb.85.7 — SET domain
Family Family familyb.85.7.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id2igqA00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology270 — Beta-clip-like
Homologous superfamily homologous superfamily10 — SET domain
Domain ID domain_id2igqB00
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)