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- PDB-1hl9: CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE IN COMP... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hl9 | ||||||
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Title | CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE IN COMPLEX WITH A MECHANISM BASED INHIBITOR | ||||||
![]() | PUTATIVE ALPHA-L-FUCOSIDASE | ||||||
![]() | HYDROLASE / GLYCOSIDE HYDROLASE / ALPHA-L-FUCOSIDASE / GLYCOSYL-ENZYME INTERMEDIATE / THERMOSTABLE | ||||||
Function / homology | ![]() alpha-L-fucosidase activity / fucose metabolic process / glycoside catabolic process / lysosome Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sulzenbacher, G. / Bignon, C. / Bourne, Y. / Henrissat, B. | ||||||
![]() | ![]() Title: Crystal Structure of Thermotoga Maritima {Alpha}-L-Fucosidase: Insights Into the Catalytic Mechanism and the Molecular Basis for Fucosidosis Authors: Sulzenbacher, G. / Bignon, C. / Nishimura, T. / Tarling, C.A. / Withers, S.G. / Henrissat, B. / Bourne, Y. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 189.3 KB | Display | ![]() |
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PDB format | ![]() | 151.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 465.2 KB | Display | ![]() |
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Full document | ![]() | 475.9 KB | Display | |
Data in XML | ![]() | 32.8 KB | Display | |
Data in CIF | ![]() | 46.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1hl8SC ![]() 1oduC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.67846, -0.73296, -0.04956), Vector: |
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Components
#1: Protein | Mass: 52315.051 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: ORF TM0306 / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Sugar | #3: Water | ChemComp-HOH / | Compound details | ALPHA-L-FUCOSIDASE BELONGS TO GLYCOSYL HYDROLASASE FAMILY 29. THE ENZYME PERFORMS CATALYSIS WITH ...ALPHA-L-FUCOSIDASE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47 % |
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Crystal grow | pH: 8 Details: 18% PEG600, 5% JEFFAMINE M600, 100 MM TRIS-HCL PH 8.0, PROTEIN CONCENTRATION 5 MG/ML THE INHIBITOR WAS INTRODUCED BY SHORT SOAKING OF A NATIVE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Mar 11, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→55.9 Å / Num. obs: 37238 / % possible obs: 89.4 % / Redundancy: 4.2 % / Rmerge(I) obs: 0.065 / Net I/σ(I): 7.1 |
Reflection shell | Resolution: 2.25→2.31 Å / Redundancy: 4 % / Rmerge(I) obs: 0.397 / Mean I/σ(I) obs: 1.8 / % possible all: 89.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1HL8 Resolution: 2.25→20 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.936 / SU B: 6.362 / SU ML: 0.159 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.411 / ESU R Free: 0.242 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. TWO OVERLAPPING SPECIES ARE PRESENT IN THE ACTIVE SITE AND HAVE BEEN REFINED WITH PARTIAL OCCUPANCIES.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.26 Å2
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Refinement step | Cycle: LAST / Resolution: 2.25→20 Å
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Refine LS restraints |
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