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- PDB-1xrb: S-adenosylmethionine synthetase (MAT, ATP: L-methionine S-adenosy... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xrb | ||||||
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Title | S-adenosylmethionine synthetase (MAT, ATP: L-methionine S-adenosyltransferase, E.C.2.5.1.6) in which MET residues are replaced with selenomethionine residues (MSE) | ||||||
![]() | S-ADENOSYLMETHIONINE SYNTHETASE | ||||||
![]() | TRANSFERASE / METHYLTRANSFERASE | ||||||
Function / homology | ![]() methionine adenosyltransferase / methionine adenosyltransferase activity / S-adenosylmethionine cycle / S-adenosylmethionine biosynthetic process / potassium ion binding / one-carbon metabolic process / magnesium ion binding / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Takusagawa, F. / Kamitori, S. / Misaki, S. / Markham, G.D. | ||||||
![]() | ![]() Title: Crystal structure of S-adenosylmethionine synthetase. Authors: Takusagawa, F. / Kamitori, S. / Misaki, S. / Markham, G.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 97.9 KB | Display | ![]() |
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PDB format | ![]() | 76.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 386.8 KB | Display | ![]() |
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Full document | ![]() | 401.6 KB | Display | |
Data in XML | ![]() | 10.5 KB | Display | |
Data in CIF | ![]() | 15.3 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: GLY 13 - HIS 14 OMEGA = 147.84 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: ASP 173 - ASP 174 OMEGA = 215.56 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: ASP 194 - GLN 195 OMEGA = 212.02 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: GLY 228 - ARG 229 OMEGA = 238.48 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: GLY 259 - GLY 260 OMEGA = 227.75 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | ||||||||
Components on special symmetry positions |
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Details | THE TETRAMERIC ENZYME CAN BE GENERATED BY THE FOLLOWING CRYSTALLOGRAPHIC SYMMETRY OPERATIONS: X, Y, Z, -X, Y-X, 1/3-Z -X, 1-Y, Z X, 1+X-Y, 1/3-Z |
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Components
#1: Protein | Mass: 42289.363 Da / Num. of mol.: 1 / Mutation: MET RESIDUES ARE REPLACED WITH SELENOMETHIONINE / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P04384, UniProt: P0A817*PLUS, methionine adenosyltransferase | ||||
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#2: Chemical | #3: Chemical | #4: Chemical | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.96 Å3/Da / Density % sol: 68.96 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 26 ℃ / pH: 7 / Method: unknown | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 3→10 Å / Num. obs: 62929 / Observed criterion σ(I): 0 |
Reflection | *PLUS Num. obs: 13507 / % possible obs: 97.7 % / Num. measured all: 62929 / Rmerge(I) obs: 0.069 |
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Processing
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Refinement | Resolution: 3→10 Å / σ(I): 2.77
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Refinement step | Cycle: LAST / Resolution: 3→10 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_dihedral_angle_deg / Dev ideal: 25.8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 3 Å / Lowest resolution: 3.13 Å / Total num. of bins used: 8 / Num. reflection obs: 1604 / Rfactor obs: 0.279 |