+Open data
-Basic information
Entry | Database: PDB / ID: 1rez | |||||||||
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Title | HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX | |||||||||
Components | LYSOZYME | |||||||||
Keywords | HYDROLASE (O-GLYCOSYL) / GLYCOSYDASE / VERTEBRATE C-TYPE | |||||||||
Function / homology | Function and homology information metabolic process / cytolysis / antimicrobial humoral response / retina homeostasis / Antimicrobial peptides / specific granule lumen / azurophil granule lumen / tertiary granule lumen / lysozyme / lysozyme activity ...metabolic process / cytolysis / antimicrobial humoral response / retina homeostasis / Antimicrobial peptides / specific granule lumen / azurophil granule lumen / tertiary granule lumen / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium / defense response to bacterium / inflammatory response / Amyloid fiber formation / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / identical protein binding Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | |||||||||
Authors | Muraki, M. / Harata, K. / Sugita, N. / Sato, K. | |||||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Origin of carbohydrate recognition specificity of human lysozyme revealed by affinity labeling. Authors: Muraki, M. / Harata, K. / Sugita, N. / Sato, K. #1: Journal: Biochemistry / Year: 1992 Title: Dissection of the Functional Role of Structural Elements of Tyrosine-63 in the Catalytic Action of Human Lysozyme Authors: Muraki, M. / Harata, K. / Jigami, Y. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rez.cif.gz | 37.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rez.ent.gz | 27.6 KB | Display | PDB format |
PDBx/mmJSON format | 1rez.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1rez_validation.pdf.gz | 441.8 KB | Display | wwPDB validaton report |
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Full document | 1rez_full_validation.pdf.gz | 442.8 KB | Display | |
Data in XML | 1rez_validation.xml.gz | 4.3 KB | Display | |
Data in CIF | 1rez_validation.cif.gz | 6.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/re/1rez ftp://data.pdbj.org/pub/pdb/validation_reports/re/1rez | HTTPS FTP |
-Related structure data
Related structure data | 1rexC 1reyC 1lz1S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14720.693 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: HUMAN LYSOZYME, PH 4.5, N-ACETYLLACTOSAMINE COVALENTLY ATTACHED TO ASP 53 VIA AN ESTER BOND Source: (natural) Homo sapiens (human) / References: UniProt: P00695, UniProt: P61626*PLUS, lysozyme |
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#2: Polysaccharide | beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
#3: Chemical | ChemComp-GOL / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.98 Å3/Da / Density % sol: 37 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.5 / Details: pH 4.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting dropDetails: Muraki, M., (1991) Biochim. Biophys. Acta 1079, 229. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ROTATING ANODE / Type: ENRAF-NONIUS FR571 / Wavelength: 1.5418 |
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Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.61→14.7 Å / Num. obs: 12070 / % possible obs: 76.9 % / Observed criterion σ(I): 0 / Redundancy: 1.3 % / Rmerge(I) obs: 0.049 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: NATIVE HUMAN LYSOZYME (PDB ENTRY 1LZ1) Resolution: 1.7→8 Å / σ(F): 3
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Displacement parameters | Biso mean: 20.74 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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