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Open data
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Basic information
Entry | Database: PDB / ID: 1oxm | ||||||
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Title | STRUCTURE OF CUTINASE | ||||||
![]() | CUTINASE | ||||||
![]() | SERINE ESTERASE / HYDROLASE / GLYCOPROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Longhi, S. / Cambillau, C. | ||||||
![]() | ![]() Title: Crystal structure of cutinase covalently inhibited by a triglyceride analogue. Authors: Longhi, S. / Mannesse, M. / Verheij, H.M. / De Haas, G.H. / Egmond, M. / Knoops-Mouthuy, E. / Cambillau, C. #1: ![]() Title: Dynamics of Fusarium Solani Cutinase Investigated Through Structural Comparison Among Different Crystal Forms of its Variants Authors: Longhi, S. / Nicolas, A. / Creveld, L. / Egmond, M. / Verrips, C.T. / De Vlieg, J. / Martinez, C. / Cambillau, C. #2: ![]() Title: Contribution of Cutinase Serine 42 Side Chain to the Stabilization of the Oxyanion Transition State Authors: Nicolas, A. / Egmond, M. / Verrips, C.T. / De Vlieg, J. / Longhi, S. / Cambillau, C. / Martinez, C. #3: ![]() Title: Cutinase, a Lipolytic Enzyme with a Preformed Oxyanion Hole Authors: Martinez, C. / Nicolas, A. / Van Tilbeurgh, H. / Egloff, M.P. / Cudrey, C. / Verger, R. / Cambillau, C. #4: ![]() Title: Fusarium Solani Cutinase is a Lipolytic Enzyme with a Catalytic Serine Accessible to Solvent Authors: Martinez, C. / De Geus, P. / Lauwereys, M. / Matthyssens, G. / Cambillau, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 107.6 KB | Display | ![]() |
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PDB format | ![]() | 86.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 953.9 KB | Display | ![]() |
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Full document | ![]() | 957.3 KB | Display | |
Data in XML | ![]() | 19.2 KB | Display | |
Data in CIF | ![]() | 26.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1cusS 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.62389, -0.46433, -0.62862), Vector: Details | THERE ARE TWO MOLECULES PER ASYMMETRIC UNIT. | |
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Components
#1: Protein | Mass: 22278.953 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P00590, Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | WT CUTINASE COVALENTLY INHIBITED BY THE TRIGLYCERIDE ANALOGUE TC4 BOUND TO THE CATALYTIC SERINE ...WT CUTINASE COVALENTLY | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 42 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 / Details: PEG 6000 IN HEPES 0.1 M PH 7, pH 7.0 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / Details: Abergel, C., (1990) J. Mol. Biol., 215, 215. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 291 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. obs: 15569 / % possible obs: 93.8 % / Observed criterion σ(I): 0 / Redundancy: 2.94 % / Rmerge(I) obs: 0.0523 / Net I/σ(I): 25.13 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.1768 / Mean I/σ(I) obs: 6.9 / % possible all: 67.7 |
Reflection | *PLUS Num. measured all: 45670 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NATIVE STRUCTURE AT 1.6 ANGSTROMS (PDB ENTRY 1CUS) Resolution: 2.3→30 Å / Cross valid method: R-FREE / σ(F): 0 Details: THE CATALYTIC SER 120 OF BOTH MOLECULES IN THE ASYMMETRIC UNIT LIES IN AN UNFAVORABLE REGION OF THE RAMACHANDRAN PLOT (EPSILON CONFORMATION) WHICH IS TYPICAL OF ALL MEMBERS OF THE ALPHA/BETA ...Details: THE CATALYTIC SER 120 OF BOTH MOLECULES IN THE ASYMMETRIC UNIT LIES IN AN UNFAVORABLE REGION OF THE RAMACHANDRAN PLOT (EPSILON CONFORMATION) WHICH IS TYPICAL OF ALL MEMBERS OF THE ALPHA/BETA HYDROLASE SUPERFAMILY.
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Refine analyze | Luzzati coordinate error obs: 0.15 Å / Luzzati sigma a obs: 0.28 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→30 Å
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Refine LS restraints |
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