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Open data
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Basic information
Entry | Database: PDB / ID: 1vhe | ||||||
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Title | Crystal structure of a aminopeptidase/glucanase homolog | ||||||
![]() | aminopeptidase/glucanase homolog | ||||||
![]() | Structural genomics / unknown function | ||||||
Function / homology | ![]() Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases / aminopeptidase activity / metallopeptidase activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Structural GenomiX | ||||||
![]() | ![]() Title: Structural analysis of a set of proteins resulting from a bacterial genomics project Authors: Badger, J. / Sauder, J.M. / Adams, J.M. / Antonysamy, S. / Bain, K. / Bergseid, M.G. / Buchanan, S.G. / Buchanan, M.D. / Batiyenko, Y. / Christopher, J.A. / Emtage, S. / Eroshkina, A. / ...Authors: Badger, J. / Sauder, J.M. / Adams, J.M. / Antonysamy, S. / Bain, K. / Bergseid, M.G. / Buchanan, S.G. / Buchanan, M.D. / Batiyenko, Y. / Christopher, J.A. / Emtage, S. / Eroshkina, A. / Feil, I. / Furlong, E.B. / Gajiwala, K.S. / Gao, X. / He, D. / Hendle, J. / Huber, A. / Hoda, K. / Kearins, P. / Kissinger, C. / Laubert, B. / Lewis, H.A. / Lin, J. / Loomis, K. / Lorimer, D. / Louie, G. / Maletic, M. / Marsh, C.D. / Miller, I. / Molinari, J. / Muller-Dieckmann, H.J. / Newman, J.M. / Noland, B.W. / Pagarigan, B. / Park, F. / Peat, T.S. / Post, K.W. / Radojicic, S. / Ramos, A. / Romero, R. / Rutter, M.E. / Sanderson, W.E. / Schwinn, K.D. / Tresser, J. / Winhoven, J. / Wright, T.A. / Wu, L. / Xu, J. / Harris, T.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 91.3 KB | Display | ![]() |
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PDB format | ![]() | 70.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 424.4 KB | Display | ![]() |
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Full document | ![]() | 426.6 KB | Display | |
Data in XML | ![]() | 18.1 KB | Display | |
Data in CIF | ![]() | 27.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1o60C ![]() 1o61C ![]() 1o62C ![]() 1o63C ![]() 1o64C ![]() 1o65C ![]() 1o66C ![]() 1o67C ![]() 1o68C ![]() 1o69C ![]() 1o6bC ![]() 1o6cC ![]() 1o6dC ![]() 1vgtC ![]() 1vguC ![]() 1vgvC ![]() 1vgwC ![]() 1vgxC ![]() 1vgyC ![]() 1vgzC ![]() 1vh0C ![]() 1vh1C ![]() 1vh2C ![]() 1vh3C ![]() 1vh4C ![]() 1vh5C ![]() 1vh6C ![]() 1vh7C ![]() 1vh8C ![]() 1vh9C ![]() 1vhaC ![]() 1vhcC ![]() 1vhdC ![]() 1vhfC ![]() 1vhgC ![]() 1vhjC ![]() 1vhkC ![]() 1vhlC ![]() 1vhmC ![]() 1vhoC ![]() 1vhqC ![]() 1vhsC ![]() 1vhtC ![]() 1vhuC ![]() 1vhvC ![]() 1vhwC ![]() 1vhxC ![]() 1vhyC ![]() 1vhzC ![]() 1vi0C ![]() 1vi1C ![]() 1vi2C ![]() 1vi3C ![]() 1vi4C ![]() 1vi5C ![]() 1vi6C ![]() 1vi8C ![]() 1vi9C ![]() 1viaC ![]() 1vicC ![]() 1vimC ![]() 1viqC ![]() 1visC ![]() 1viuC ![]() 1vivC ![]() 1vixC ![]() 1viyC ![]() 1vizC 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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 41188.043 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.84 Å3/Da / Density % sol: 56.71 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() | |||||||||
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Detector | Type: MARRESEARCH / Detector: CCD | |||||||||
Radiation | Protocol: MAD / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 1.9→45.72 Å / Num. all: 38362 / Num. obs: 38362 / % possible obs: 99.9 % / Redundancy: 41.84 % / Rmerge(I) obs: 0.13 / Net I/σ(I): 34.7 | |||||||||
Reflection shell | Resolution: 1.9→1.97 Å / Rmerge(I) obs: 0.292 / Mean I/σ(I) obs: 13.1 / % possible all: 99.3 | |||||||||
Reflection | *PLUS Redundancy: 41.8 % / Rmerge(I) obs: 0.13 | |||||||||
Reflection shell | *PLUS % possible obs: 99.3 % |
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Processing
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Refinement | Method to determine structure: Se-Met MAD phasing / Resolution: 1.9→45.72 Å / σ(F): 0
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Solvent computation | Solvent model: Babinet bulk solvent correction / Bsol: 418.204 Å2 / ksol: 0.992 e/Å3 | ||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 10.954 Å2
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Refine Biso | Class: all / Treatment: isotropic | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→45.72 Å
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Refine LS restraints |
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Software | *PLUS Version: 4 / Classification: refinement | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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