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- PDB-1ffr: CRYSTAL STRUCTURE OF CHITINASE A MUTANT Y390F COMPLEXED WITH HEXA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ffr | |||||||||
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Title | CRYSTAL STRUCTURE OF CHITINASE A MUTANT Y390F COMPLEXED WITH HEXA-N-ACETYLCHITOHEXAOSE (NAG)6 | |||||||||
![]() | CHITINASE A | |||||||||
![]() | HYDROLASE / TIM BARREL / PROTEIN-OLIGOSACCHARIDE COMPLEX | |||||||||
Function / homology | ![]() chitinase / chitinase activity / chitin catabolic process / chitin binding / polysaccharide catabolic process / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Papanikolau, Y. / Prag, G. / Tavlas, G. / Vorgias, C.E. / Oppenheim, A.B. / Petratos, K. | |||||||||
![]() | ![]() Title: High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis. Authors: Papanikolau, Y. / Prag, G. / Tavlas, G. / Vorgias, C.E. / Oppenheim, A.B. / Petratos, K. #1: ![]() Title: CDE NOVO PURIFICATION SCHEME AND CRYSTALLIZATION CONDITIONS YIELD HIGH-RESOLUTION STRUCTURES OF CHITINASE A AND ITS COMPLEX WITH THE INHIBITOR ALLOSAMIDIN Authors: Papanikolau, Y. / Tavlas, G. / Vorgias, C.E. / Petratos, K. #2: ![]() Title: Crystal Structure of a bacterial chitinase at 2.3 Angstrom resolution Authors: Perrakis, A. / Tews, I. / Dauter, Z. / Oppenheim, A.B. / Chet, I. / Wilson, K.S. / Vorgias, C.E. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 140.2 KB | Display | ![]() |
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PDB format | ![]() | 105 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 748.2 KB | Display | ![]() |
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Full document | ![]() | 760.5 KB | Display | |
Data in XML | ![]() | 31 KB | Display | |
Data in CIF | ![]() | 48.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ehnC ![]() 1eibC ![]() 1edqS C: citing same article ( S: Starting model for refinement |
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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: 58623.590 Da / Num. of mol.: 1 / Mutation: Y390F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: GenBank: AB015996, UniProt: P07254*PLUS, chitinase |
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#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(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 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.25 Å3/Da / Density % sol: 62 % | ||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.2 Details: 0.75 M CITRATE-NA AND 20% (V/V) METHANOL, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18-20 ℃ | ||||||||||||||||||||
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: MARRESEARCH / Detector: CCD / Date: Apr 17, 2000 / Details: PAIR OF NICKEL MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→10 Å / Num. all: 68036 / Num. obs: 68036 / % possible obs: 93.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Biso Wilson estimate: 22 Å2 / Rmerge(I) obs: 0.061 / Net I/σ(I): 23.4 |
Reflection shell | Resolution: 1.8→1.86 Å / Rmerge(I) obs: 0.204 / Mean I/σ(I) obs: 6.2 / Num. unique all: 6945 / % possible all: 96.8 |
Reflection | *PLUS |
Reflection shell | *PLUS % possible obs: 96.8 % / Redundancy: 2.9 % / Rmerge(I) obs: 0.18 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1EDQ Resolution: 1.8→10 Å / SU B: 2.39 / SU ML: 0.08 / σ(F): 0 / σ(I): 0 / ESU R: 0.12 / ESU R Free: 0.12 / Stereochemistry target values: Engh & Huber Details: THE CLOSE CONTACT LISTED IN REMARK 500 IS DUE TO THE RESULT OF AVERAGING OF TWO CO-EXISTING STRUCTURES WITH UNCLEAVED AND CLEAVED BOND BETWEEN ATOMS O4 AND C1 OF THE SUGAR RESIDUES
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Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / σ(F): 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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