9rtn

State 2 MAP 2 SPT6 with SETD2

Method: ELECTRON MICROSCOPY Dmax: 123.5 Å Quality: GOOD

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

RNA polymerase II subunit D

OrganismNot specified

UniProt A0A287ADR4

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 43–184 Not recorded DNA-directed RNA polymerase II subunit RPB7 × 1 (A0A4X1VKG7) Histone-lysine N-methyltransferase SETD2 × 1 (Q9BYW2) Transcription elongation factor SPT5 × 1 (O00267) Transcription elongation factor SPT6 × 1 (Q7KZ85) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.82 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.

58 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A287ADR4_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–142; UniProt 43–184

DNA-directed RNA polymerase II subunit RPB7

OrganismNot specified

UniProt A0A4X1VKG7

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 1–172 Not recorded RNA polymerase II subunit D × 1 (A0A287ADR4) Histone-lysine N-methyltransferase SETD2 × 1 (Q9BYW2) Transcription elongation factor SPT5 × 1 (O00267) Transcription elongation factor SPT6 × 1 (Q7KZ85) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.82 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.

83 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A4X1VKG7_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–172; UniProt 1–172

Histone-lysine N-methyltransferase SETD2

Homo sapiens

UniProt Q9BYW2

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain O; UniProt 1435–2564 Not recorded RNA polymerase II subunit D × 1 (A0A287ADR4) DNA-directed RNA polymerase II subunit RPB7 × 1 (A0A4X1VKG7) Transcription elongation factor SPT5 × 1 (O00267) Transcription elongation factor SPT6 × 1 (Q7KZ85) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.82 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.

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

View Construct and Data Evidence
UniProt name SETD2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain O; PDBConstruct 4–1133; UniProt 1435–2564

Transcription elongation factor SPT5

Homo sapiens

UniProt O00267

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain Z; UniProt 1–1087 Not recorded RNA polymerase II subunit D × 1 (A0A287ADR4) DNA-directed RNA polymerase II subunit RPB7 × 1 (A0A4X1VKG7) Histone-lysine N-methyltransferase SETD2 × 1 (Q9BYW2) Transcription elongation factor SPT6 × 1 (Q7KZ85) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.82 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.

53 other PDB entries and 57 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPT5H_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain Z; PDBConstruct 1–1087; UniProt 1–1087

Transcription elongation factor SPT6

Homo sapiens

UniProt Q7KZ85

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain M; UniProt 1–1726 Not recorded RNA polymerase II subunit D × 1 (A0A287ADR4) DNA-directed RNA polymerase II subunit RPB7 × 1 (A0A4X1VKG7) Histone-lysine N-methyltransferase SETD2 × 1 (Q9BYW2) Transcription elongation factor SPT5 × 1 (O00267) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.82 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.

24 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPT6H_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain M; PDBConstruct 4–1729; UniProt 1–1726

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 9rtn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9rtn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9rtn
Deposition date deposition_date2025-07-03
Structure title titleState 2 MAP 2 SPT6 with SETD2
Keywords keywordsRNA Pol II Activated elongation complex Co-transcriptional H3K36me3 SETD2, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.86
Radius of gyration Rg (electron density) rg_electron38.09
Forward intensity I(0) i0417803000.00
Molecular weight molecular_weight166420.0 kDa
Excluded volume excluded_volume208650 ų
Envelope volume envelope_volume294330 ų
Hydration-shell volume shell_volume63472 ų
Envelope diameter envelope_diameter129.3
Shell Rg shell_rg44.84
Envelope Rg envelope_rg37.44
Shape Rg shape_rg38.09
Total Rg total_rg38.50
Total atoms total_atoms23362
Residues n_residues1447
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 dmax123.5
Rg (real space) rg_real38.62
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real4.1780e+08
I(0) uncertainty (real space) i0_real_error7.9530e+06
Rg (reciprocal space) rg_reciprocal38.77
I(0) (reciprocal space) i0_reciprocal417900000.0000
Solution quality estimate total_estimate0.8972
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.140
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46870000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)