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- PDB-1c82: MECHANISM OF HYALURONAN BINDING AND DEGRADATION: STRUCTURE OF STR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1c82 | |||||||||
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Title | MECHANISM OF HYALURONAN BINDING AND DEGRADATION: STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE IN COMPLEX WITH HYALURONIC ACID DISACCHARIDE AT 1.7 A RESOLUTION | |||||||||
![]() | HYALURONATE LYASE | |||||||||
![]() | LYASE / PROTEIN-CARBOHYDRATE COMPLEX | |||||||||
Function / homology | ![]() hyaluronate lyase / hyaluronate lyase activity / hydrolase activity, acting on glycosyl bonds / carbohydrate binding / carbohydrate metabolic process / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Ponnuraj, K. / Jedrzejas, M.J. | |||||||||
![]() | ![]() Title: Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 A resolution. Authors: Ponnuraj, K. / Jedrzejas, M.J. #1: ![]() Title: Structural Basis of Hyaluronan Degradation by Streptococcus pneumoniae Hyaluronate Lyase Authors: Li, S. / Kelly, S.J. / Lamani, E. / Ferraroni, M. / Jedrzejas, M.J. | |||||||||
History |
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Remark 999 | SEQUENCE THE SIX RESIDUE HIS TAG WAS NOT SEEN IN THE DENSITY. THE ELECTRON DENSITY OF RESIDUE 731 ...SEQUENCE THE SIX RESIDUE HIS TAG WAS NOT SEEN IN THE DENSITY. THE ELECTRON DENSITY OF RESIDUE 731 SUGGESTS IT IS A VALINE. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 172.6 KB | Display | ![]() |
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PDB format | ![]() | 131.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 83561.938 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||||
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#2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.7 % | ||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: evaporation / pH: 6 Details: AMMONIUM SULFATE, SODIUM CACODYLATE, pH 6.0, EVAPORATION, temperature 293K | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: OXFORD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→100 Å / Num. all: 495691 / Num. obs: 95261 / % possible obs: 98.5 % / Redundancy: 5.2 % / Rmerge(I) obs: 0.055 / Net I/σ(I): 23.4 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.336 / Num. unique all: 9367 / % possible all: 98 |
Reflection | *PLUS Num. measured all: 495691 |
Reflection shell | *PLUS % possible obs: 98 % / Mean I/σ(I) obs: 4.9 |
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Processing
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Refinement | Resolution: 1.7→40 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.7→40 Å
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Refine LS restraints | Type: x_bond_d / Dev ideal: 0.009 | ||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refine LS restraints | *PLUS
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