[English] 日本語
Yorodumi- PDB-7o4g: Human phosphomannomutase 2 (PMM2) wild-type soaked with the activ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7o4g | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Human phosphomannomutase 2 (PMM2) wild-type soaked with the activator glucose 1,6-bisphosphate | |||||||||
Components | Phosphomannomutase 2 | |||||||||
Keywords | ISOMERASE / glycobiology / congenital disorders of glycosylation / phosphotransferase / phosphomutase | |||||||||
Function / homology | Function and homology information Defective PMM2 causes PMM2-CDG / Synthesis of GDP-mannose / phosphomannomutase / phosphomannomutase activity / GDP-mannose biosynthetic process / mannose metabolic process / protein N-linked glycosylation / protein glycosylation / neuronal cell body / nucleoplasm ...Defective PMM2 causes PMM2-CDG / Synthesis of GDP-mannose / phosphomannomutase / phosphomannomutase activity / GDP-mannose biosynthetic process / mannose metabolic process / protein N-linked glycosylation / protein glycosylation / neuronal cell body / nucleoplasm / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.66 Å | |||||||||
Authors | Ramon-Maiques, S. / Briso-Montiano, A. / Del Cano-Ochoa, F. / Vilas, A. / Perez, B. / Rubio, V. | |||||||||
Funding support | Spain, 2items
| |||||||||
Citation | Journal: J Inherit Metab Dis / Year: 2022 Title: Insight on molecular pathogenesis and pharmacochaperoning potential in phosphomannomutase 2 deficiency, provided by novel human phosphomannomutase 2 structures. Authors: Briso-Montiano, A. / Del Cano-Ochoa, F. / Vilas, A. / Velazquez-Campoy, A. / Rubio, V. / Perez, B. / Ramon-Maiques, S. | |||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 7o4g.cif.gz | 235.3 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb7o4g.ent.gz | 154.9 KB | Display | PDB format |
PDBx/mmJSON format | 7o4g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o4/7o4g ftp://data.pdbj.org/pub/pdb/validation_reports/o4/7o4g | HTTPS FTP |
---|
-Related structure data
Related structure data | 7o0cSC 7o1bC 7o58C 7o5zC S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||
Unit cell |
| ||||||||||||
Components on special symmetry positions |
|
-Components
-Protein / Sugars , 2 types, 3 molecules AB
#1: Protein | Mass: 28274.336 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: Residues GPMAAP at the N-terminus are not seen in the electron density map. The most N-terminal GP sequence is part of the fusion tag after cleavage Source: (gene. exp.) Homo sapiens (human) / Gene: PMM2 / Plasmid: pOPIN-B / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O15305, phosphomannomutase #5: Sugar | ChemComp-G16 / | |
---|
-Non-polymers , 5 types, 82 molecules
#2: Chemical | ChemComp-GOL / | ||||||
---|---|---|---|---|---|---|---|
#3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-CL / | #6: Chemical | ChemComp-NA / | #7: 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: 2.4 Å3/Da / Density % sol: 46.5 % Description: Crystals of hexagonal morphology and 0.025 mm in the largest dimension |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: Drops made by mixing 1 microliter of protein solution and 1 microliter of crystallization deposit solution. Protein solution contained 5 mg/ml protein in 20 mM Hepes pH 7.5 and 0.2 M NaCl. ...Details: Drops made by mixing 1 microliter of protein solution and 1 microliter of crystallization deposit solution. Protein solution contained 5 mg/ml protein in 20 mM Hepes pH 7.5 and 0.2 M NaCl. Crystallization solution contained 0.3-0.4 M MgCl2, 24% PEG3350 and 0.1 M HEPES pH 7.5. Crystals were soaked for 5-10 min in mother liquor with 6 mM glucose 1,6-bisphophate. |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 0.97926 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 19, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97926 Å / Relative weight: 1 |
Reflection | Resolution: 2.66→361.27 Å / Num. obs: 16779 / % possible obs: 100 % / Redundancy: 25.3 % / Biso Wilson estimate: 52.66 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.417 / Rpim(I) all: 0.085 / Net I/σ(I): 9.2 |
Reflection shell | Resolution: 2.66→2.79 Å / Redundancy: 26.7 % / Rmerge(I) obs: 3.011 / Mean I/σ(I) obs: 1.8 / Num. unique obs: 2150 / CC1/2: 0.625 / Rpim(I) all: 0.813 / % possible all: 100 |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 7O0C Resolution: 2.66→60.21 Å / SU ML: 0.2639 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 24.7825 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
| |||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 49.98 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.66→60.21 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|