6kiw

Cryo-EM structure of human MLL3-ubNCP complex (4.0 angstrom)

Method: ELECTRON MICROSCOPY Dmax: 157.2 Å Quality: GOOD

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

Histone H3

Xenopus laevis

UniProt A0A310TTQ1

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–DNA Heteromer Protein × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (144-MER) × 1 DNA (145-MER) × 1 Histone-lysine N-methyltransferase 2C × 1 (Q8NEZ4) Retinoblastoma-binding protein 5 × 1 (Q15291) Ubiquitin × 1 (P62979) WD repeat-containing protein 5 × 1 (P61964) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 Å

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.

126 other PDB entries and 130 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A310TTQ1_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

Histone H4

Xenopus laevis

UniProt P62799

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–DNA Heteromer Protein × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (144-MER) × 1 DNA (145-MER) × 1 Histone-lysine N-methyltransferase 2C × 1 (Q8NEZ4) Retinoblastoma-binding protein 5 × 1 (Q15291) Ubiquitin × 1 (P62979) WD repeat-containing protein 5 × 1 (P61964) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 Å

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.

354 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103

Histone H2A

Xenopus laevis

UniProt Q6AZJ8

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–DNA Heteromer Protein × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (144-MER) × 1 DNA (145-MER) × 1 Histone-lysine N-methyltransferase 2C × 1 (Q8NEZ4) Retinoblastoma-binding protein 5 × 1 (Q15291) Ubiquitin × 1 (P62979) WD repeat-containing protein 5 × 1 (P61964) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 Å

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.

226 other PDB entries and 238 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6AZJ8_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

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–DNA Heteromer Protein × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Mutation:S29T/K117C Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) DNA (144-MER) × 1 DNA (145-MER) × 1 Histone-lysine N-methyltransferase 2C × 1 (Q8NEZ4) Retinoblastoma-binding protein 5 × 1 (Q15291) Ubiquitin × 1 (P62979) WD repeat-containing protein 5 × 1 (P61964) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 Å

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.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–122; UniProt 5–126 Author chain H; PDBConstruct 1–122; UniProt 5–126

Histone-lysine N-methyltransferase 2C

Homo sapiens

UniProt Q8NEZ4

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–DNA Heteromer Protein × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain K; UniProt 4707–4911 Mutation:C4708S Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (144-MER) × 1 DNA (145-MER) × 1 Retinoblastoma-binding protein 5 × 1 (Q15291) Ubiquitin × 1 (P62979) WD repeat-containing protein 5 × 1 (P61964) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 Å

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.

8 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KMT2C_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–205; UniProt 4707–4911

Retinoblastoma-binding protein 5

Homo sapiens

UniProt Q15291

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–DNA Heteromer Protein × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain N; UniProt 1–538 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (144-MER) × 1 DNA (145-MER) × 1 Histone-lysine N-methyltransferase 2C × 1 (Q8NEZ4) Ubiquitin × 1 (P62979) WD repeat-containing protein 5 × 1 (P61964) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 Å

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.

31 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBBP5_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain N; PDBConstruct 1–538; UniProt 1–538

Ubiquitin

Homo sapiens

UniProt P62979

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–DNA Heteromer Protein × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain O; UniProt 1–76 Mutation:G76C Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (144-MER) × 1 DNA (145-MER) × 1 Histone-lysine N-methyltransferase 2C × 1 (Q8NEZ4) Retinoblastoma-binding protein 5 × 1 (Q15291) WD repeat-containing protein 5 × 1 (P61964) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 Å

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.

221 other PDB entries and 235 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS27A_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain O; PDBConstruct 1–76; UniProt 1–76

WD repeat-containing protein 5

Homo sapiens

UniProt P61964

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–DNA Heteromer Protein × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain R; UniProt 1–334 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (144-MER) × 1 DNA (145-MER) × 1 Histone-lysine N-methyltransferase 2C × 1 (Q8NEZ4) Retinoblastoma-binding protein 5 × 1 (Q15291) Ubiquitin × 1 (P62979) Set1/Ash2 histone methyltransferase complex subunit ASH2 × 1 (Q9UBL3) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 Å

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.

198 other PDB entries and 294 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR5_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain R; PDBConstruct 1–334; UniProt 1–334

Set1/Ash2 histone methyltransferase complex subunit ASH2

Homo sapiens

UniProt Q9UBL3

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–DNA Heteromer Protein × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain T; UniProt 95–628 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (144-MER) × 1 DNA (145-MER) × 1 Histone-lysine N-methyltransferase 2C × 1 (Q8NEZ4) Retinoblastoma-binding protein 5 × 1 (Q15291) Ubiquitin × 1 (P62979) WD repeat-containing protein 5 × 1 (P61964) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 Å

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.

31 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASH2L_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain T; PDBConstruct 1–534; UniProt 95–628

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 6kiw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6kiw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6kiw
Deposition date deposition_date2019-07-20
Structure title titleCryo-EM structure of human MLL3-ubNCP complex (4.0 angstrom)
Keywords keywordshistone modification, nucleosome, MLL, TRANSCRIPTION, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.19
Radius of gyration Rg (electron density) rg_electron48.25
Forward intensity I(0) i01803210000.00
Molecular weight molecular_weight292850.0 kDa
Excluded volume excluded_volume341480 ų
Envelope volume envelope_volume544540 ų
Hydration-shell volume shell_volume92292 ų
Envelope diameter envelope_diameter160.8
Shell Rg shell_rg54.67
Envelope Rg envelope_rg46.73
Shape Rg shape_rg48.23
Total Rg total_rg48.52
Total atoms total_atoms20225
Residues n_residues2098
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 dmax157.2
Rg (real space) rg_real48.86
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real1.8030e+09
I(0) uncertainty (real space) i0_real_error3.6160e+07
Rg (reciprocal space) rg_reciprocal49.19
I(0) (reciprocal space) i0_reciprocal1804000000.0000
Solution quality estimate total_estimate0.8829
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.8
Skewness Skewness skewness0.118
Kurtosis Kurtosis kurtosis-0.440
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha183200000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.871

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id6kiwA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6kiwB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6kiwC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6kiwD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6kiwE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6kiwF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6kiwG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6kiwH00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6kiwK01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology270 — Beta-clip-like
Homologous superfamily homologous superfamily10 — SET domain
Domain ID domain_id6kiwN01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id6kiwR00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id6kiwT00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily920 — SPRY domain

8. Citations (1)

9. Files and Curves (10)