1pqv

RNA polymerase II-TFIIS complex

Method: X-RAY DIFFRACTION Dmax: 171.6 Å Quality: GOOD

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

DNA-directed RNA polymerase II largest subunit

OrganismNot specified

UniProt P04050

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain A; UniProt 1–1733 Not recorded DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

211 other PDB entries and 218 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1733; UniProt 1–1733

DNA-directed RNA polymerase II 140 kDa polypeptide

OrganismNot specified

UniProt P08518

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain B; UniProt 1–1224 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

195 other PDB entries and 202 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1224; UniProt 1–1224

DNA-directed RNA polymerase II 45 kDa polypeptide

OrganismNot specified

UniProt P16370

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain C; UniProt 1–318 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

193 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB3_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–318; UniProt 1–318

DNA-directed RNA polymerase II 32 kDa polypeptide

OrganismNot specified

UniProt P20433

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain D; UniProt 1–221 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

103 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB4_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–221; UniProt 1–221

DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide

OrganismNot specified

UniProt P20434

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain E; UniProt 1–215 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

264 other PDB entries and 277 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB5_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–215; UniProt 1–215

DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide

OrganismNot specified

UniProt P20435

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain F; UniProt 1–155 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

280 other PDB entries and 293 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB6_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–155; UniProt 1–155

DNA-directed RNA polymerase II 19 kDa polypeptide

OrganismNot specified

UniProt P34087

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain G; UniProt 1–171 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

104 other PDB entries and 108 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB7_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–171; UniProt 1–171

DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide

OrganismNot specified

UniProt P20436

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain H; UniProt 1–146 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

264 other PDB entries and 277 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB8_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–146; UniProt 1–146

DNA-directed RNA polymerase II 14.2 kDa polypeptide

OrganismNot specified

UniProt P27999

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain I; UniProt 1–122 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

192 other PDB entries and 199 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB9_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–122; UniProt 1–122

DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide

OrganismNot specified

UniProt P22139

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain J; UniProt 1–70 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

263 other PDB entries and 276 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB10_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–70; UniProt 1–70

DNA-directed RNA polymerase II 13.6 kDa polypeptide

OrganismNot specified

UniProt P38902

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain K; UniProt 1–120 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

193 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPB11_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–120; UniProt 1–120

DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide

OrganismNot specified

UniProt P40422

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain L; UniProt 1–70 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) Transcription elongation factor S-II × 1 (P07273) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

263 other PDB entries and 276 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPC10_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain L; PDBConstruct 1–70; UniProt 1–70

Transcription elongation factor S-II

OrganismNot specified

UniProt P07273

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain S; UniProt 1–309 Not recorded DNA-directed RNA polymerase II largest subunit × 1 (P04050) DNA-directed RNA polymerase II 140 kDa polypeptide × 1 (P08518) DNA-directed RNA polymerase II 45 kDa polypeptide × 1 (P16370) DNA-directed RNA polymerase II 32 kDa polypeptide × 1 (P20433) DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide × 1 (P20434) DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide × 1 (P20435) DNA-directed RNA polymerase II 19 kDa polypeptide × 1 (P34087) DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide × 1 (P20436) DNA-directed RNA polymerase II 14.2 kDa polypeptide × 1 (P27999) DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide × 1 (P22139) DNA-directed RNA polymerase II 13.6 kDa polypeptide × 1 (P38902) DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide × 1 (P40422) MG MAGNESIUM ION × 1 ZN ZINC ION × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;sodium-ammonium tartrate, Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.80 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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TFS2_YEAST
Isoform
PDB entities 13
Chains and sequence ranges Author chain S; PDBConstruct 1–309; UniProt 1–309

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 1pqv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1pqv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1pqv
Deposition date deposition_date2003-06-19
Structure title titleRNA polymerase II-TFIIS complex
Keywords keywords;TRANSCRIPTION, MRNA CLEAVAGE, PROOFREADING, BACKTRACKING, GENE EXPRESSION, MULTIPROTEIN COMPLEX, PROTEIN SOAKING, TRANSFERASE-TRANSCRIPTION COMPLEX ;; TRANSFERASE/TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier51.94
Radius of gyration Rg (electron density) rg_electron51.57
Forward intensity I(0) i02976540000.00
Molecular weight molecular_weight456220.0 kDa
Excluded volume excluded_volume561060 ų
Envelope volume envelope_volume577620 ų
Hydration-shell volume shell_volume95680 ų
Envelope diameter envelope_diameter172.2
Shell Rg shell_rg54.74
Envelope Rg envelope_rg48.88
Shape Rg shape_rg51.50
Total Rg total_rg51.65
Total atoms total_atoms10
Residues n_residues
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 dmax171.6
Rg (real space) rg_real51.78
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real2.9760e+09
I(0) uncertainty (real space) i0_real_error5.7660e+07
Rg (reciprocal space) rg_reciprocal52.07
I(0) (reciprocal space) i0_reciprocal2978000000.0000
Solution quality estimate total_estimate0.8744
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.9
Skewness Skewness skewness0.222
Kurtosis Kurtosis kurtosis-0.381
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha310900000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.877

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

7. Fold Classification (SCOP + CATH) 13 domains

SCOP 2.08 (13 domains)

Domain ID domain_idd1pqva_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvb_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvc_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvd_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqve_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvf_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvg_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvh_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvi_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvj_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvk_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvl_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase
Domain ID domain_idd1pqvs_
Class classi — Low resolution protein structures
Fold Fold foldi.8 — RNA polymerase
Superfamily Superfamily superfamilyi.8.1 — RNA polymerase
Family Family familyi.8.1.1 — RNA polymerase

8. Citations (2)

9. Files and Curves (10)