SAXSdb — 3mqm

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

Probable histone-lysine N-methyltransferase ASH1L

Homo sapiens

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 2438–2564	Fragment：BROMODOMAIN of human ASH1L (UNP RESIDUES 2438:2564)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.15M NaNO3 20% PEG3350 10% EtGly, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.54 Å R-free 0.259
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 2438–2564	Fragment：BROMODOMAIN of human ASH1L (UNP RESIDUES 2438:2564)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.15M NaNO3 20% PEG3350 10% EtGly, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.54 Å R-free 0.259
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 2438–2564 Chain B； UniProt 2438–2564	Fragment：BROMODOMAIN of human ASH1L (UNP RESIDUES 2438:2564)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.15M NaNO3 20% PEG3350 10% EtGly, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.54 Å R-free 0.259

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.

Other PDB	Difference from Current Entry 3MQM	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3OPE Structural Basis of Auto-inhibitory mechanism of Histone methyltransferase Deposited 2010-08-31	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2074–2293（220 aa） Fragment：SET domain (UNP RESIDUES 2074-2293)	Not recorded	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；Bistrisprofane, PEG, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.90 Å R-free 0.299
3OPE Structural Basis of Auto-inhibitory mechanism of Histone methyltransferase Deposited 2010-08-31	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2074–2293（220 aa） Fragment：SET domain (UNP RESIDUES 2074-2293)	Not recorded	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；Bistrisprofane, PEG, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.90 Å R-free 0.299
4YNM ASH1L wild-type SET domain in complex with S-adenosyl methionine (SAM) Deposited 2015-03-10	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Not recorded	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris	Resolution 2.19 Å R-free 0.278
4YNM ASH1L wild-type SET domain in complex with S-adenosyl methionine (SAM) Deposited 2015-03-10	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Not recorded	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris	Resolution 2.19 Å R-free 0.278
4YNP ASH1L SET domain S2259M mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Mutation：S2259M	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris	Resolution 2.90 Å R-free 0.319
4YNP ASH1L SET domain S2259M mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Mutation：S2259M	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris	Resolution 2.90 Å R-free 0.319
4YPA ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Mutation：Q2265A	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290 K；PEG 4000, magnesium chloride, Tris	Resolution 2.30 Å R-free 0.303
4YPA ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Mutation：Q2265A	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290 K；PEG 4000, magnesium chloride, Tris	Resolution 2.30 Å R-free 0.303
4YPA ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Mutation：Q2265A	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290 K；PEG 4000, magnesium chloride, Tris	Resolution 2.30 Å R-free 0.303
4YPA ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Mutation：Q2265A	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290 K；PEG 4000, magnesium chloride, Tris	Resolution 2.30 Å R-free 0.303
4YPE ASH1L SET domain H2193F mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Mutation：H2193F	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris	Resolution 2.20 Å R-free 0.263
4YPE ASH1L SET domain H2193F mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Mutation：H2193F	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mM Tris	Resolution 2.20 Å R-free 0.263
4YPU ASH1L SET domain K2264L mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Mutation：K2264L	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mm Tris	Resolution 2.60 Å R-free 0.305
4YPU ASH1L SET domain K2264L mutant in complex with S-adenosyl methionine (SAM) Deposited 2015-03-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2074–2293（220 aa） Fragment：SET domain (UNP residues 2074-2293)	Mutation：K2264L	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；PEG 3350, 20 mm Tris	Resolution 2.60 Å R-free 0.305
6AGO Crystal structure of MRG15-ASH1L Histone methyltransferase complex Deposited 2018-08-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2039–2293（255 aa）	Not recorded	SAM S-ADENOSYLMETHIONINE × 1 ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；295 K；Ammonium Acetate	Resolution 3.10 Å R-free 0.272
6AGO Crystal structure of MRG15-ASH1L Histone methyltransferase complex Deposited 2018-08-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 2039–2293（255 aa）	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；295 K；Ammonium Acetate	Resolution 3.10 Å R-free 0.272
6INE Crystal Structure of human ASH1L-MRG15 complex Deposited 2018-10-25	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2026–2288（263 aa）	Not recorded	ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；0.1 M Tris-HCl pH 8.5, 20 % PEG 6000, 0.2 M Trimethylamine-N-oxide	Resolution 2.60 Å R-free 0.237
6WZW Ash1L SET domain in complex with AS-85 Deposited 2020-05-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2074–2293（220 aa）	Not recorded	EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 SAM S-ADENOSYLMETHIONINE × 1 ZN ZINC ION × 3 UG7 N-{[3-(3-carbamothioylphenyl)-1-{1-[(trifluoromethyl)sulfonyl]piperidin-4-yl}-1H-indol-6-yl]methyl}azetidine-3-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；290 K；0.1 M HEPES pH 7.5, 30% PEG3350	Resolution 1.69 Å R-free 0.206
6X0P Ash1L SET domain Q2265A mutant in complex with AS-5 Deposited 2020-05-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2074–2293（220 aa）	Mutation：Q2265A	UK7 3-[6-(aminomethyl)-1-(2-hydroxyethyl)-1H-indol-3-yl]benzene-1-carbothioamide × 1 ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG4000	Resolution 1.69 Å R-free 0.213
6X0P Ash1L SET domain Q2265A mutant in complex with AS-5 Deposited 2020-05-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2074–2293（220 aa）	Mutation：Q2265A	UK7 3-[6-(aminomethyl)-1-(2-hydroxyethyl)-1H-indol-3-yl]benzene-1-carbothioamide × 1 ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG4000	Resolution 1.69 Å R-free 0.213
6X0P Ash1L SET domain Q2265A mutant in complex with AS-5 Deposited 2020-05-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 2074–2293（220 aa）	Mutation：Q2265A	UK7 3-[6-(aminomethyl)-1-(2-hydroxyethyl)-1H-indol-3-yl]benzene-1-carbothioamide × 1 ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG4000	Resolution 1.69 Å R-free 0.213
6X0P Ash1L SET domain Q2265A mutant in complex with AS-5 Deposited 2020-05-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 2074–2293（220 aa）	Mutation：Q2265A	UK7 3-[6-(aminomethyl)-1-(2-hydroxyethyl)-1H-indol-3-yl]benzene-1-carbothioamide × 1 ZN ZINC ION × 3 SAM S-ADENOSYLMETHIONINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG4000	Resolution 1.69 Å R-free 0.213
7Y0I Solution structures of ASH1L PHD domain in complex with H3K4me2 peptide Deposited 2022-06-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2584–2635（52 aa）	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 7.2；298 K；Ionic strength (raw mmCIF value) null；Pressure 1 NMR sample composition 50 mM sodium phosphate, 100 mM sodium chloride, 100 uM ZINC ION, 2.0 mM [U-100% 2H] DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 50 mM sodium phosphate, 100 mM sodium chloride, 100 uM ZINC ION, 2.0 mM [U-100% 2H] DTT, 100% D2O \| 100% D2O	Resolution not provided
8VLD Crystal structure of Ash1L PHD finger in complex with histone H3K4me2 Deposited 2024-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2584–2636（53 aa） Chain B 2584–2636（53 aa）	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1.6 M sodium citrate pH 6.5	Resolution 1.92 Å R-free 0.249
8VLF Crystal structure of Ash1L PHD finger in complex with histone H3K4me3 Deposited 2024-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2584–2636（53 aa） Chain B 2584–2636（53 aa）	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1.6 M sodium citrate pH 6.5	Resolution 1.34 Å R-free 0.188
8VLH Crystal structure of Ash1L PHD-BAH domains Deposited 2024-01-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2584–2839（256 aa） Chain B 2584–2839（256 aa）	Not recorded	ZN ZINC ION × 4 SR STRONTIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1 M Bis-Tris propane pH 10, 0.25 M strontium chloride, 0.01 M ammonium sulfate, and 25% PEG 8000	Resolution 2.40 Å R-free 0.284

14 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ASH1L_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–126； UniProt 2438–2564 Author chain B； PDBConstruct 3–126； UniProt 2438–2564

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3mqm
Deposition date deposition_date	2010-04-28
Structure title title	Crystal Structure of the Bromodomain of human ASH1L
Keywords keywords	;ASH1L, Ash1, KIAA1420, Absent small and homeotic disks protein 1 homolog, Lysine N-methyltransferase 2H, KMT2H, Structural Genomics Consortium, SGC, TRANSFERASE ;; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	20.73 Å
Radius of gyration Rg (electron density) rg_electron	19.90 Å
Forward intensity I(0) i0	12835300.00
Molecular weight molecular_weight	27194.0 kDa
Excluded volume excluded_volume	34195 Å³
Envelope volume envelope_volume	41644 Å³
Hydration-shell volume shell_volume	18150 Å³
Envelope diameter envelope_diameter	76.0 Å
Shell Rg shell_rg	25.64 Å
Envelope Rg envelope_rg	20.03 Å
Shape Rg shape_rg	19.89 Å
Total Rg total_rg	20.81 Å
Total atoms total_atoms	1918
Residues n_residues	252
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	71.5 Å
Rg (real space) rg_real	20.71 Å
Rg uncertainty (real space) rg_real_error	0.63 Å
I(0) (real space) i0_real	1.2840e+07
I(0) uncertainty (real space) i0_real_error	1.6830e+05
Rg (reciprocal space) rg_reciprocal	20.72 Å
I(0) (reciprocal space) i0_reciprocal	12840000.0000
Solution quality estimate total_estimate	0.7928
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	24.9 Å
Skewness Skewness skewness	0.342
Kurtosis Kurtosis kurtosis	-0.195
Angular range angular_range	— – 0.3850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2251000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.776; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3mqma1
Class class	a — All alpha proteins
Fold Fold fold	a.29 — Bromodomain-like
Superfamily Superfamily superfamily	a.29.2 — Bromodomain
Family Family family	a.29.2.0 — automated matches

Domain ID domain_id	d3mqma2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3mqmb1
Class class	a — All alpha proteins
Fold Fold fold	a.29 — Bromodomain-like
Superfamily Superfamily superfamily	a.29.2 — Bromodomain
Family Family family	a.29.2.0 — automated matches

Domain ID domain_id	d3mqmb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id	3mqmA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily	10 — Bromodomain-like

Domain ID domain_id	3mqmB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily	10 — Bromodomain-like

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8. Citations (1)

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Unit-cell length a length_a	69.590 Å
Unit-cell length b length_b	69.590 Å
Unit-cell length c length_c	151.340 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 65
Space-group number int_tables_number	170
Crystal system crystal_system	—

Resolution resolution	2.540 Å
Low-resolution limit resolution_low	47.140 Å
R factor r_factor	0.2070
R_work r_work	0.2040
R_free r_free	0.2590

Description description	Probable histone-lysine N-methyltransferase ASH1L
Molecular weight formula_weight	14375.5 kDa
EC 编号 ec_number	2.1.1.43
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	1933

Crystal Structure of the Bromodomain of human ASH1L

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

Probable histone-lysine N-methyltransferase ASH1L

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	15

fit	/app/data/saxs_computation/mq/3mqm/3mqm.fit
pddf	/app/data/pr_computation/mq/3mqm/3mqm.pr.out
profile	/app/data/saxs_computation/mq/3mqm/3mqm.dat