Current Protein Identity:Q07794
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 2RIM Crystal structure of Rtt109 Deposited 2007-10-12 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
1–436(436 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 8.5;298 K;PEG550 MME, Ammonium citrate, glycerol, Tris, pH8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.20 Å R-free 0.259 |
| 2RIM Crystal structure of Rtt109 Deposited 2007-10-12 | Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
1–436(436 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 8.5;298 K;PEG550 MME, Ammonium citrate, glycerol, Tris, pH8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.20 Å R-free 0.259 |
| 2ZFN Self-acetylation mediated histone H3 lysine 56 acetylation by rtt109 Deposited 2008-01-08 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
1–436(436 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | ACO ACETYL COENZYME *A × 1 GOL GLYCEROL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;PEG, Tris, Ammonium citrate, glycerol, ethylene glycol, pH8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 1.90 Å R-free 0.229 |
| 3CZ7 Molecular Basis for the Autoregulation of the Protein Acetyl Transferase Rtt109 Deposited 2008-04-28 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
1–127(127 aa)
Chain A
171–403(233 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) | ACO ACETYL COENZYME *A × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 4.4;294 K;12% (w/v) PEG 4,000, 1 mM ZnCl2, and 100 mM Sodium Acetate, pH 4.4, temperature 294K, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.00 Å R-free 0.189 |
| 3Q33 Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation Deposited 2010-12-21 | Assembly 1 Protein heterocomplex Heteromer;Protein × 6 PDB declaration: hexameric(6) Consistent with protein count |
Chain A
1–436(436 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | ACO ACETYL COENZYME *A × 2 EDO 1,2-ETHANEDIOL × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 7.5;298 K;10.0% (v/v) PEG 8000
8% (v/v) ethylene glycol
100 mM Hepes, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.5
|
Resolution 2.80 Å R-free 0.255 |
| 3Q35 Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation Deposited 2010-12-21 | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count |
Chain A
1–436(436 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | ACO ACETYL COENZYME *A × 2 EDO 1,2-ETHANEDIOL × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;10.0% (v/v) PEG8000;
8% (v/v) ethylene glycol;
100 mM Hepes, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.5
|
Resolution 3.30 Å R-free 0.248 |
| 3Q66 Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P6122) Deposited 2010-12-30 | Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count |
Chain C
1–436(436 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | SO4 SULFATE ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;0.1 M sodium citrate tribasic dihydrate, 2 M ammonium sulfate, 0.2 M potassium sodium tartrate tetrahydrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K
|
Resolution 2.71 Å R-free 0.247 |
| 3Q68 Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P212121) Deposited 2010-12-30 | Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count |
Chain C
1–436(436 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;1.8 M sodium citrate, 30% (w/v) 1,6-hexanediol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K
|
Resolution 2.71 Å R-free 0.226 |
| 3QM0 Crystal structure of RTT109-AC-CoA complex Deposited 2011-02-03 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
1–129(129 aa)
Fragment:RTT109 DELTA(130-179)
Chain A
180–436(257 aa)
Fragment:RTT109 DELTA(130-179)
|
Mutation:DELTA(130-179) mutant Non-standard monomer:Yes (specific site not provided by mmCIF) Mutation:DELTA(130-179) mutant Non-standard monomer:Yes (specific site not provided by mmCIF) | HG MERCURY (II) ION × 2 ACO ACETYL COENZYME *A × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;reservoir solution contains 12.5% (v/v) PEG4000, 100 mM Hepes. Protein (10 mg/ml) in 20 mM Hepes, 150 mM NaCl, and 5 mM BME, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.10 Å R-free 0.258 |
| 6O22 Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate. Deposited 2019-02-22 | Assembly 1 Protein heterocomplex Heteromer;Protein × 6 PDB declaration: hexameric(6) Consistent with protein count |
Chain C
1–436(436 aa)
|
Not recorded | No recorded non-water small molecule | Not declared |
NMR measurement conditions
pH 6.5;298 K;Ionic strength (raw mmCIF value) 150;Pressure 1
NMR sample composition
70 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 70 uM Rtt109, 70 uM Asf1, 70 uM H3, 70 uM H4, 100% D2O | 100% D2O
NMR sample composition
70 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 70 uM Rtt109, 70 uM Asf1, 70 uM H3(110A,63C) mutant with a cysteine coupled to a paramagnetic tag, 70 uM H4, 100% D2O | 100% D2O
NMR sample composition
90 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 90 uM Rtt109, 90 uM Asf1, 90 uM H3(110A,76C) mutant with a cysteine coupled to a paramagnetic tag, 90 uM H4, 100% D2O | 100% D2O
NMR sample composition
30 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 30 uM Rtt109, 30 uM Asf1, 30 uM H3, 30 uM H4(30C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O | 100% D2O
NMR sample composition
70 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 70 uM Rtt109, 70 uM Asf1, 70 uM H3, 70 uM H4(82C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O | 100% D2O
NMR sample composition
80 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 80 uM Rtt109, 80 uM Asf1, 80 uM H3, 80 uM H4(45C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O | 100% D2O
NMR sample composition
30 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 30 uM Rtt109, 30 uM Asf1, 30 uM H3, 30 uM H4(93C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O | 100% D2O
|
Resolution not provided |