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- PDB-1mda: CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mda | ||||||
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Title | CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN | ||||||
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![]() | ELECTRON TRANSPORT | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Chen, L. / Durley, R. / Mathews, F.S. | ||||||
![]() | ![]() Title: Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin. Authors: Chen, L. / Durley, R. / Poliks, B.J. / Hamada, K. / Chen, Z. / Mathews, F.S. / Davidson, V.L. / Satow, Y. / Huizinga, E. / Vellieux, F.M. / Hol, W.G.J. #1: ![]() Title: Three-Dimensional Structure of the Quinoprotein Methylamine Dehydrogenase from Paracoccus Denitrificans Determined by Molecular Replacement at 2.8 Angstroms Resolution Authors: Chen, L. / Mathews, F.S. / Davidson, V.L. / Huizinga, E.G. / Vellieux, F.M.D. / Hol, W.G.J. #2: ![]() Title: A New Cofactor in a Prokaryotic Enzyme: Tryptophan Tryptophylquinone as the Redox Prosthetic Group in Methylamine Dehydrogenase Authors: Mcintire, W.S. / Wemmer, D.E. / Chistoserdov, A. / Lidstrom, M.E. #3: ![]() Title: Structure of Quinoprotein Methylamine Dehydrogenase at 2.25 Angstroms Resolution Authors: Vellieux, F.M.D. / Huitema, F. / Groendijk, H. / Kalk, K.H. / Frank Jzn., J. / Jongejan, J.A. / Duine, J.A. / Petratos, K. / Drenth, J. / Hol, W.G.J. #4: ![]() Title: Structure Determination of Quinoprotein Methylamine Dehydrogenase from Thiobacillus Versutus Authors: Vellieux, F.M.D. / Kalk, K.H. / Drenth, J. / Hol, W.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 | ![]() | 214.1 KB | Display | ![]() |
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PDB format | ![]() | 167.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 416.9 KB | Display | ![]() |
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Full document | ![]() | 546 KB | Display | |
Data in XML | ![]() | 41.5 KB | Display | |
Data in CIF | ![]() | 59.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Atom site foot note | 1: CIS PROLINE - PRO A 6 / 2: CIS PROLINE - PRO B 6 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.3439, -0.7653, -0.5441), Vector: Details | THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *H* AND *L* WHEN APPLIED TO CHAIN *J* AND *M*, RESPECTIVELY. | |
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Components
#1: Protein | Mass: 36866.598 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Protein | Mass: 13080.426 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #3: Protein | Mass: 11260.903 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #4: Chemical | ChemComp-CU / Compound details | THE REDOX CENTERS OF MADH ARE LOCATED ON EACH L SUBUNIT. EACH IS COMPOSED OF THE SIDE CHAINS OF TWO ...THE REDOX CENTERS OF MADH ARE LOCATED ON EACH L SUBUNIT. EACH IS COMPOSED OF THE SIDE CHAINS OF TWO AMINO ACIDS ON THE L SUBUNIT, BOTH ARE TRYPTOPHAN | Sequence details | THIS IS AN X-RAY DETERMINED SEQUENCE WHICH WAS ESTABLISHED ON THE BASIS OF THE ELECTRON DENSITY DUE ...THIS IS AN X-RAY DETERMINED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.93 Å3/Da / Density % sol: 68.67 % | |||||||||||||||
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Crystal grow | *PLUS pH: 6.5 / Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.5 Å / Rmerge(I) obs: 0.084 |
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Processing
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Refinement | Rfactor obs: 0.285 / Highest resolution: 2.5 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.5 Å / Rfactor obs: 0.285 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 45 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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