+Open data
-Basic information
Entry | Database: PDB / ID: 5ab0 | |||||||||
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Title | Crystal structure of aminopeptidase ERAP2 with ligand | |||||||||
Components |
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Keywords | HYDROLASE / AMINOPEPTIDASE / ERAP2 / ZINC ION BINDING / ENDOPLASMIC RETICULUM / METALLOPROTEASE / L-RAP / ANTIGEN PRESENTATION | |||||||||
Function / homology | Function and homology information Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases / antigen processing and presentation of peptide antigen via MHC class I / peptide catabolic process / metalloaminopeptidase activity / aminopeptidase activity / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / peptide binding / antigen processing and presentation of endogenous peptide antigen via MHC class I / regulation of blood pressure / metallopeptidase activity ...Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases / antigen processing and presentation of peptide antigen via MHC class I / peptide catabolic process / metalloaminopeptidase activity / aminopeptidase activity / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / peptide binding / antigen processing and presentation of endogenous peptide antigen via MHC class I / regulation of blood pressure / metallopeptidase activity / endopeptidase activity / adaptive immune response / endoplasmic reticulum lumen / endoplasmic reticulum membrane / proteolysis / extracellular space / zinc ion binding / membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | HOMO SAPIENS (human) SYNTHETIC CONSTRUCT (others) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | |||||||||
Authors | Mpakali, A. / Giastas, P. / Saridakis, E. / Stratikos, E. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2015 Title: Structural Basis for Antigenic Peptide Recognition and Processing by Endoplasmic Reticulum (Er) Aminopeptidase 2. Authors: Mpakali, A. / Giastas, P. / Mathioudakis, N. / Mavridis, I.M. / Saridakis, E. / Stratikos, E. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ab0.cif.gz | 397.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ab0.ent.gz | 320.8 KB | Display | PDB format |
PDBx/mmJSON format | 5ab0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5ab0_validation.pdf.gz | 2.4 MB | Display | wwPDB validaton report |
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Full document | 5ab0_full_validation.pdf.gz | 2.4 MB | Display | |
Data in XML | 5ab0_validation.xml.gz | 72.6 KB | Display | |
Data in CIF | 5ab0_validation.cif.gz | 99.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/5ab0 ftp://data.pdbj.org/pub/pdb/validation_reports/ab/5ab0 | HTTPS FTP |
-Related structure data
Related structure data | 5ab2C 5cu5C 4e36S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
-Protein / Protein/peptide , 2 types, 4 molecules ACEF
#1: Protein | Mass: 111563.422 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) References: UniProt: Q6P179, leucyl aminopeptidase, aminopeptidase B #2: Protein/peptide | Mass: 1313.528 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others) |
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-Sugars , 4 types, 16 molecules
#3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Polysaccharide | Source method: isolated from a genetically manipulated source #5: Polysaccharide | beta-D-mannopyranose-(1-4)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...beta-D-mannopyranose-(1-4)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #7: Sugar | ChemComp-NAG / |
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-Non-polymers , 4 types, 410 molecules
#6: Chemical | #8: Chemical | ChemComp-EDO / #9: Chemical | ChemComp-MES / | #10: Water | ChemComp-HOH / | |
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-Details
Sequence details | CORRESPOND |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 38.45 % / Description: NONE |
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Crystal grow | pH: 6.3 Details: 6 %(W/V) PEG MW 8000, 25 %(V/V) ETHYLENE GLYCOL, 59 MM MES AND 41 MM IMIDAZOLE AT PH 6.3 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 1 |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Nov 30, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→65.7 Å / Num. obs: 88335 / % possible obs: 99.5 % / Observed criterion σ(I): 1.6 / Redundancy: 3.7 % / Biso Wilson estimate: 54.5 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 6 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.81 / Mean I/σ(I) obs: 1.6 / % possible all: 99.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4E36 Resolution: 2.5→65.726 Å / SU ML: 0.37 / σ(F): 1.33 / Phase error: 27.84 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 56.3 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→65.726 Å
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Refine LS restraints |
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LS refinement shell |
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