[English] 日本語
Yorodumi- PDB-7ms6: Structure of USP5 zinc-finger ubiquitin binding domain co-crystal... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7ms6 | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of USP5 zinc-finger ubiquitin binding domain co-crystallized with (2-fluoro-4-((4-phenylpiperidin-1-yl)sulfonyl)benzoyl)glycine | ||||||
Components | Ubiquitin carboxyl-terminal hydrolase 5 | ||||||
Keywords | HYDROLASE/INHIBITOR / USP5 / ubiquitin / USP / ubiquitin specific protease / HYDROLASE / HYDROLASE-INHIBITOR complex | ||||||
Function / homology | Function and homology information protein K48-linked deubiquitination / negative regulation of ubiquitin-dependent protein catabolic process / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / ubiquitin binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / lysosome / protein ubiquitination / Ub-specific processing proteases ...protein K48-linked deubiquitination / negative regulation of ubiquitin-dependent protein catabolic process / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / ubiquitin binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / lysosome / protein ubiquitination / Ub-specific processing proteases / cysteine-type endopeptidase activity / proteolysis / zinc ion binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 1.55 Å | ||||||
Authors | Mann, M.K. / Zepeda-Velazquez, C.A. / Alvarez, H.G. / Dong, A. / Kiyota, T. / Aman, A. / Arrowsmith, C.H. / Al-Awar, R. / Harding, R.J. / Schapira, M. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2021 Title: Structure-Activity Relationship of USP5 Inhibitors. Authors: Mann, M.K. / Zepeda-Velazquez, C.A. / Gonzalez-Alvarez, H. / Dong, A. / Kiyota, T. / Aman, A.M. / Loppnau, P. / Li, Y. / Wilson, B. / Arrowsmith, C.H. / Al-Awar, R. / Harding, R.J. / Schapira, M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 7ms6.cif.gz | 44.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb7ms6.ent.gz | 27.1 KB | Display | PDB format |
PDBx/mmJSON format | 7ms6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ms/7ms6 ftp://data.pdbj.org/pub/pdb/validation_reports/ms/7ms6 | HTTPS FTP |
---|
-Related structure data
Related structure data | 7ms5C 7ms7C 6nftS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 13535.199 Da / Num. of mol.: 1 / Fragment: UNP residues 171-290 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: USP5, ISOT / Production host: Escherichia coli (E. coli) / References: UniProt: P45974, ubiquitinyl hydrolase 1 |
---|
-Non-polymers , 5 types, 141 molecules
#2: Chemical | ChemComp-ZPV / |
---|---|
#3: Chemical | ChemComp-SO4 / |
#4: Chemical | ChemComp-EDO / |
#5: Chemical | ChemComp-ZN / |
#6: Water | ChemComp-HOH / |
-Details
Has ligand of interest | Y |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.11 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop Details: 2 M ammonium sulfate, 0.2 M sodium acetate, 0.1 M HEPES pH 7.5, 5% MPD |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU FR-E SUPERBRIGHT / Wavelength: 1.54178 Å | ||||||||||||||||||||||||||||||
Detector | Type: RIGAKU SATURN A200 / Detector: CCD / Date: Nov 2, 2020 | ||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||
Reflection | Resolution: 1.55→38.1 Å / Num. obs: 22155 / % possible obs: 99.3 % / Redundancy: 7.8 % / CC1/2: 0.998 / Rmerge(I) obs: 0.044 / Rpim(I) all: 0.016 / Rrim(I) all: 0.047 / Net I/σ(I): 33.5 | ||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
|
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: 6NFT Resolution: 1.55→38.07 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.953 / SU B: 0.833 / SU ML: 0.031 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.059 / ESU R Free: 0.058 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 61.82 Å2 / Biso mean: 12.457 Å2 / Biso min: 6.72 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.55→38.07 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.55→1.59 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
|