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- PDB-1bpm: DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BIN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1bpm | ||||||
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Title | DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY | ||||||
![]() | LEUCINE AMINOPEPTIDASE | ||||||
![]() | HYDROLASE(ALPHA-AMINOACYLPEPTIDE) | ||||||
Function / homology | ![]() cysteinylglycine-S-conjugate dipeptidase / prolyl aminopeptidase / leucyl aminopeptidase / dipeptidase activity / metalloaminopeptidase activity / carboxypeptidase activity / disordered domain specific binding / peptidase activity / manganese ion binding / mitochondrion ...cysteinylglycine-S-conjugate dipeptidase / prolyl aminopeptidase / leucyl aminopeptidase / dipeptidase activity / metalloaminopeptidase activity / carboxypeptidase activity / disordered domain specific binding / peptidase activity / manganese ion binding / mitochondrion / proteolysis / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kim, H. / Lipscomb, W.N. | ||||||
![]() | ![]() Title: Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography. Authors: Kim, H. / Lipscomb, W.N. #1: ![]() Title: Structure Determination and Refinement of Bovine Lens Leucine Aminopeptidase and its Complex with Bestatin Authors: Burley, S.K. / David, P.R. / Sweet, R.M. / Taylor, A. / Lipscomb, W.N. #2: ![]() Title: Molecular Structure of Leucine Aminopeptidase at 2.7-Angstroms Resolution Authors: Burley, S.K. / David, P.R. / Taylor, A. / Lipscomb, W.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 101.1 KB | Display | ![]() |
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PDB format | ![]() | 78.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 369.7 KB | Display | ![]() |
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Full document | ![]() | 389.5 KB | Display | |
Data in XML | ![]() | 13.1 KB | Display | |
Data in CIF | ![]() | 19.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Atom site foot note | 1: RESIDUE 471 IS A CIS PROLINE. |
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Components
#1: Protein | Mass: 52942.098 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.73 Å3/Da / Density % sol: 54.92 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 30 Å / Num. obs: 13523 / % possible obs: 98 % / Rmerge(I) obs: 0.162 / Num. measured all: 134829 |
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Processing
Software | Name: ![]() | ||||||||||||
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Refinement | Rfactor Rwork: 0.189 / Highest resolution: 2.9 Å Details: ONE OF THE ACTIVE SITE ZINC IONS HAS BEEN REPLACED BY A MAGNESIUM ION AS DETERMINED FROM X-RAY DIFFRACTION DATA COLLECTED AT -150 DEGREES C. | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.9 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 10 Å / Num. reflection obs: 10797 / σ(I): 2 / Rfactor obs: 0.189 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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