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- PDB-2mta: CRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2mta | |||||||||
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Title | CRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE, AMICYANIN AND A C-TYPE CYTOCHROME | |||||||||
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![]() | ELECTRON TRANSPORT | |||||||||
Function / homology | ![]() methanol metabolic process / methylamine dehydrogenase (amicyanin) / methylamine dehydrogenase (amicyanin) activity / methylamine metabolic process / aliphatic amine dehydrogenase activity / amine metabolic process / outer membrane-bounded periplasmic space / periplasmic space / electron transfer activity / iron ion binding ...methanol metabolic process / methylamine dehydrogenase (amicyanin) / methylamine dehydrogenase (amicyanin) activity / methylamine metabolic process / aliphatic amine dehydrogenase activity / amine metabolic process / outer membrane-bounded periplasmic space / periplasmic space / electron transfer activity / iron ion binding / copper ion binding / heme binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Chen, L. / Mathews, F.S. | |||||||||
![]() | ![]() Title: Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i. Authors: Chen, L. / Durley, R.C. / Mathews, F.S. / Davidson, V.L. #1: ![]() Title: Crystal Structure Analysis of Amicyanin and Apoamicyanin from Paraccus Denitrificans at 2.0 Angstroms and 1.8 Angstroms Resolution Authors: Durley, R. / Chen, L. / Lim, L.W. / Mathews, F.S. / Davidson, V.L. #2: ![]() Title: Preliminary Crystal Structure Studies of a Ternary Electron Transfer Complex between a Quinoprotein, a Blue Copper Protein, and a C-Type Cytochrome Authors: Chen, L. / Mathews, F.S. / Davidson, V.L. / Tegoni, M. / Rivetti, C. / Rossi, G.L. #3: ![]() 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.D. / Hol, W.G.J. #4: ![]() 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. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 158.3 KB | Display | ![]() |
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PDB format | ![]() | 128.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 507.2 KB | Display | ![]() |
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Full document | ![]() | 535.8 KB | Display | |
Data in XML | ![]() | 19.8 KB | Display | |
Data in CIF | ![]() | 29.6 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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1 | ![]()
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO H 145 2: GLN C 146 - PRO C 147 OMEGA =145.73 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | ||||||||
Components on special symmetry positions |
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Components
-METHYLAMINE DEHYDROGENASE ... , 2 types, 2 molecules HL
#1: Protein | Mass: 41063.945 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Protein | Mass: 13728.206 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
-Protein , 2 types, 2 molecules AC
#3: Protein | Mass: 11505.171 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#4: Protein | Mass: 16274.852 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
-Non-polymers , 4 types, 130 molecules H![](data/chem/img/PO4.gif)
A![](data/chem/img/CU.gif)
![](data/chem/img/HEC.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/CU.gif)
![](data/chem/img/HEC.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | #6: Chemical | #7: Chemical | ChemComp-HEC / | #8: Water | ChemComp-HOH / | |
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-Details
Compound details | THIS IS THE FIRST TERNARY COMPLEX COMPOSED OF THREE SEQUENTIAL PROTEINS IN AN ELECTRON TRANSFER ...THIS IS THE FIRST TERNARY COMPLEX COMPOSED OF THREE SEQUENTIAL |
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Nonpolymer details | THE REDOX COFACTOR TTQ OF MADH IS LOCATED ON EACH L SUBUNIT, WHICH IS COMPRISED OF THE SIDE CHAINS ...THE REDOX COFACTOR TTQ OF MADH IS LOCATED ON EACH L SUBUNIT, WHICH IS COMPRISED OF THE SIDE CHAINS OF TWO TRYPTOPHAN |
Sequence details | SEQUENCE ADVISORY NOTICE: AT PRESENT, THE SEQUENCE DATABASES INDICATE THAT RESIDUE 299 OF THE HEAVY ...SEQUENCE ADVISORY NOTICE: AT PRESENT, THE SEQUENCE DATABASES INDICATE THAT RESIDUE 299 OF THE HEAVY CHAIN IS LEU AND RESIDUE 300 IS LEU. THE AUTHORS FOUND THAT THEY MISREAD THE GELS AND THAT RESIDUES 299 AND 300 SHOULD BE PHE AND VAL, RESPECTIVE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 57.61 % |
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Processing
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Refinement | Rfactor Rwork: 0.179 / Rfactor obs: 0.179 / Highest resolution: 2.4 Å Details: THE CURRENT MODEL CONTAINS AN AMICYANIN PORTION TRANSFORMED FROM THE MADH-AMICYANIN BINARY COMPLEX (CHEN ET AL., BIOCHEMISTRY, 1992), WHICH WAS NOT INCLUDED IN THE PHASE REFINEMENT. ONLY THE ...Details: THE CURRENT MODEL CONTAINS AN AMICYANIN PORTION TRANSFORMED FROM THE MADH-AMICYANIN BINARY COMPLEX (CHEN ET AL., BIOCHEMISTRY, 1992), WHICH WAS NOT INCLUDED IN THE PHASE REFINEMENT. ONLY THE CA OF EACH RESIDUE AND THE COPPER ATOM ARE INCLUDED AT THIS STAGE. THE CYTOCHROME PORTION OF THE CURRENT MODEL IS SIMULATED FROM CYTOCHROME C551 DEPOSITED IN PROTEIN DATA BANK (MUTSUURA ET AL., J. MOL. BIOL. 1982). ONLY THE HEME GROUP WAS BUILT TO FIT THE ELECTRON DENSITY AND IS SUBMITTED. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.4 Å
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Refine LS restraints |
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