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Open data
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Basic information
Entry | Database: PDB / ID: 1ft7 | ||||||
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Title | AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID | ||||||
![]() | BACTERIAL LEUCYL AMINOPEPTIDASE | ||||||
![]() | HYDROLASE / zinc / peptidase / bimetallic | ||||||
Function / homology | ![]() bacterial leucyl aminopeptidase / metalloexopeptidase activity / aminopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Stamper, C. / Bennett, B. / Holz, R. / Petsko, G. / Ringe, D. | ||||||
![]() | ![]() Title: Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis. Authors: Stamper, C. / Bennett, B. / Edwards, T. / Holz, R.C. / Ringe, D. / Petsko, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 66.7 KB | Display | ![]() |
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PDB format | ![]() | 53.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 384 KB | Display | ![]() |
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Full document | ![]() | 390.6 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 12.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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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: 31427.350 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q01693, bacterial leucyl aminopeptidase | ||||||
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#2: Chemical | #3: Chemical | ChemComp-K / | #4: Chemical | ChemComp-PLU / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.12 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 Details: KSCN, NaCl, Tris, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 4 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→12 Å / Num. all: 349668 / Num. obs: 349668 / % possible obs: 75 % / Observed criterion σ(F): 10 / Observed criterion σ(I): 10 / Redundancy: 6.7 % / Biso Wilson estimate: 10 Å2 / Rmerge(I) obs: 0.18 / Net I/σ(I): 6 |
Reflection shell | Resolution: 2.17→2.2 Å / Redundancy: 3 % / Rmerge(I) obs: 0.65 / % possible all: 65 |
Reflection | *PLUS Num. obs: 21129 / % possible obs: 99.9 % / Num. measured all: 349668 / Rmerge(I) obs: 0.134 |
Reflection shell | *PLUS % possible obs: 100 % |
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Processing
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Refinement | Resolution: 2.2→10 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refine LS restraints | *PLUS
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