TRANSCRIPTION ELONGATION FACTOR S-II
Saccharomyces cerevisiae
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 1–77 | Fragment:DOMAIN I | No other associated polymer | SOLUTION NMR NMR measurement conditions:pH 7.5;273 K;Ionic strength (raw mmCIF value) 300 mM NaCl;Pressure ambient NMR sample composition:2 mM TFIIS1-111; 10 mM phosphate buffer; 90% H2O, 10%D2O | 90% H2O/10% D2O | Resolution not provided |
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 1EO0 | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1ENW ELONGATION FACTOR TFIIS DOMAIN II Deposited 2000-03-21 | Different construct Different experimental conditions | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
131–240(110 aa)
Fragment:DOMAIN II (RESIDUES 131-240)
|
Not recorded | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 6.5;270 K;Ionic strength (raw mmCIF value) 50 mM;Pressure ambient
NMR sample composition
2 mM TFIIS; 5mM phosphate buffer; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition
2 mM TFIIS; 5mM phosphate buffer; 99.996% D2O | 99.996% D2O
|
Resolution not provided |
| 1PQV RNA polymerase II-TFIIS complex Deposited 2003-06-19 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 13 PDB declaration: tridecameric |
Chain S
1–309(309 aa)
|
Not recorded | 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 |
| 1Y1V Refined RNA Polymerase II-TFIIS complex Deposited 2004-11-19 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 13 PDB declaration: tridecameric |
Chain S
131–309(179 aa)
|
Not recorded | ZN ZINC ION × 9 MG MAGNESIUM ION × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 3.80 Å R-free 0.294 |
| 1Y1Y RNA Polymerase II-TFIIS-DNA/RNA complex Deposited 2004-11-19 | Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer;Protein × 13 PDB declaration: pentadecameric |
Chain S
131–309(179 aa)
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 4.00 Å |
| 3GTM Co-complex of Backtracked RNA polymerase II with TFIIS Deposited 2009-03-27 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer;Protein × 11 PDB declaration: tetradecameric |
Chain S
147–306(160 aa)
Fragment:Transcription Factor IIS E291H mutation, UNP residues 147-309
|
Mutation:E291H | MG MAGNESIUM ION × 1 ZN ZINC ION × 9 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;390mM (NH4)2HPO4/NaH2PO4, pH 6.0, 50mM Dioxane, 10mM DTT, 9-11% PEG 6000, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.80 Å R-free 0.289 |
| 3PO3 Arrested RNA Polymerase II reactivation intermediate Deposited 2010-11-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer;Protein × 13 PDB declaration: hexadecameric |
Chain S
132–309(178 aa)
|
Mutation:D290A | ZN ZINC ION × 9 MG MAGNESIUM ION × 1 ACT ACETATE ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 PGE TRIETHYLENE GLYCOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;4-7% PEG6000, 50mM HEPES pH 7.0, 200mM AMMONIUM ACETATE, 300mM SODIUM ACETATE, 5mM TCEP
, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 3.30 Å R-free 0.189 |
| 5FMF the P-lobe of RNA polymerase II pre-initiation complex Deposited 2015-11-03 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 25 PDB declaration: 27-meric |
Chain 2
136–309(174 aa)
|
Not recorded | MG MAGNESIUM ION × 2 ZN ZINC ION × 9 |
ELECTRON MICROSCOPY
cryo-EM buffer
20 MM HEPES (PH7.6), 5 MM DTT, 2 MM MG(OAC)2,AND 40 MM KOAC;pH 7.6;20 MM HEPES (PH7.6), 5 MM DTT, 2 MM MG(OAC)2,AND 40 MM KOAC
cryo-EM vitrification conditions
Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 100, TEMPERATURE- 120, INSTRUMENT- FEI VITROBOT MARK III,
|
Resolution 6.00 Å |
| 7FAW Structure of LW domain from Yeast Deposited 2021-07-07 | Different construct Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
1–73(73 aa)
Fragment:LW domain
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;291 K;0.1M Tris, pH 8.5, 25% PEG 3350
|
Resolution 2.44 Å R-free 0.240 |
| 7FAW Structure of LW domain from Yeast Deposited 2021-07-07 | Different construct Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain B
1–73(73 aa)
Fragment:LW domain
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;291 K;0.1M Tris, pH 8.5, 25% PEG 3350
|
Resolution 2.44 Å R-free 0.240 |
| 7FAW Structure of LW domain from Yeast Deposited 2021-07-07 | Different construct Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain C
1–73(73 aa)
Fragment:LW domain
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;291 K;0.1M Tris, pH 8.5, 25% PEG 3350
|
Resolution 2.44 Å R-free 0.240 |
| 7UI9 Core Mediator-PICearly (Copy A) Deposited 2022-03-28 | Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 33 PDB declaration: 33-meric |
Chain S
1–309(309 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.6
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.30 Å |
| 7UIF Mediator-PIC Early (Core B) Deposited 2022-03-29 | Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 33 PDB declaration: 33-meric |
Chain S
1–309(309 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.6
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.60 Å |
| 7UIO Mediator-PIC Early (Composite Model) Deposited 2022-03-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 78 PDB declaration: 80-meric |
Chain AS
1–309(309 aa)
Chain BS
1–309(309 aa)
|
Not recorded | ZN ZINC ION × 4 THR THREONINE × 1 ALA ALANINE × 1 ASP ASPARTIC ACID × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.6
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.30 Å |
| 8UOQ Composite map of PIC_delta_TFIIK form2 Deposited 2023-10-20 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 28 PDB declaration: 30-meric |
Chain S
1–309(309 aa)
|
Not recorded | ZN ZINC ION × 15 MG MAGNESIUM ION × 2 SF4 IRON/SULFUR CLUSTER × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.6
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.80 Å |
| 8UOT Composite map of PICdeltaTFIIK form1 Deposited 2023-10-20 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 28 PDB declaration: 30-meric |
Chain S
1–309(309 aa)
|
Not recorded | SF4 IRON/SULFUR CLUSTER × 1 ZN ZINC ION × 15 MG MAGNESIUM ION × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.6;20 mM HEPES PH 7.6
50 mM KOAc
5 mM DTT
2 mM MgOAc
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.70 Å |
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 | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 1–77; UniProt 1–77 |