+
Open data
-
Basic information
Entry | Database: PDB / ID: 4psx | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of histone acetyltransferase complex | ||||||
![]() |
| ||||||
![]() | HISTONE/TRANSFERASE / HAT WD40 / acetyltransferase / AcCoA / Phosphorylation / HISTONE-TRANSFERASE complex | ||||||
Function / homology | ![]() sexual sporulation resulting in formation of a cellular spore / HATs acetylate histones / global genome nucleotide-excision repair / RNA polymerase I upstream activating factor complex / Rpd3L complex / Rpd3L-Expanded complex / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Assembly of the ORC complex at the origin of replication ...sexual sporulation resulting in formation of a cellular spore / HATs acetylate histones / global genome nucleotide-excision repair / RNA polymerase I upstream activating factor complex / Rpd3L complex / Rpd3L-Expanded complex / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Assembly of the ORC complex at the origin of replication / HDACs deacetylate histones / histone H4 acetyltransferase activity / NuRD complex / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / ESC/E(Z) complex / replication fork protection complex / Oxidative Stress Induced Senescence / RMTs methylate histone arginines / SUMOylation of chromatin organization proteins / positive regulation of transcription by RNA polymerase I / RNA Polymerase I Promoter Escape / nucleolar large rRNA transcription by RNA polymerase I / Estrogen-dependent gene expression / rRNA transcription / histone acetyltransferase complex / subtelomeric heterochromatin formation / CENP-A containing nucleosome / histone acetyltransferase activity / nucleosome binding / histone acetyltransferase / structural constituent of chromatin / nucleosome / nucleosome assembly / chromatin organization / histone binding / chromosome, telomeric region / chromatin remodeling / protein heterodimerization activity / DNA repair / chromatin binding / regulation of DNA-templated transcription / DNA binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Yang, M. / Li, Y. | ||||||
![]() | ![]() Title: Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex Authors: Li, Y. / Zhang, L. / Liu, T. / Chai, C. / Fang, Q. / Wu, H. / Agudelo garcia, P.A. / Han, Z. / Zong, S. / Yu, Y. / Zhang, X. / Parthun, M.R. / Chai, J. / Xu, R.M. / Yang, M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 601.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 501.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 999 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 61 KB | Display | |
Data in CIF | ![]() | 85.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4pswSC S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
|
-
Components
-Histone acetyltransferase type B ... , 2 types, 4 molecules ADBE
#1: Protein | Mass: 37566.344 Da / Num. of mol.: 2 / Fragment: UNP residues 7-319 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: HAT1, LPA16W, YP8132.12, YPL001W / Production host: ![]() ![]() #2: Protein | Mass: 45107.902 Da / Num. of mol.: 2 / Fragment: UNP residues 8-389 / Mutation: V143T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: HAT2, YEL056W / Production host: ![]() ![]() |
---|
-Protein/peptide , 2 types, 4 molecules CFYP
#3: Protein/peptide | Mass: 5093.079 Da / Num. of mol.: 2 / Fragment: UNP residues 2-49 / Mutation: I21V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: HHF1, YBR009C, YBR0122, HHF2, YNL030W, N2752 / Production host: ![]() ![]() #4: Protein/peptide | Mass: 1565.797 Da / Num. of mol.: 2 / Fragment: UNP residues 2-16 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|
-Non-polymers , 3 types, 609 molecules ![](data/chem/img/COA.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | #6: Chemical | ChemComp-SO4 / | #7: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.7 Å3/Da / Density % sol: 66.75 % |
---|---|
Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 0.2M potassium sodium tartrate, 20%(w/v) polyethylene glycol 3,350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jun 1, 2012 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→38.6 Å / Num. all: 66418 / Num. obs: 66418 / % possible obs: 75.67 % / Observed criterion σ(F): 1.98 / Observed criterion σ(I): 1.98 |
Reflection shell | Resolution: 2.5→2.55 Å / % possible all: 75.67 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 4PSW Resolution: 2.509→38.6 Å / SU ML: 0.23 / σ(F): 1.98 / Phase error: 24.6 / Stereochemistry target values: ML
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.509→38.6 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 24
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS params. | Method: refined / Origin x: -13.3471 Å / Origin y: -60.3416 Å / Origin z: -15.4922 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS group | Selection details: all |