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- PDB-1xym: THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xym | ||||||
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Title | THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID | ||||||
![]() | XYLOSE ISOMERASE![]() | ||||||
![]() | ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) | ||||||
Function / homology | ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Allen, K.N. / Lavie, A. / Petsko, G.A. / Ringe, D. | ||||||
![]() | ![]() Title: Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid. Authors: Allen, K.N. / Lavie, A. / Glasfeld, A. / Tanada, T.N. / Gerrity, D.P. / Carlson, S.C. / Farber, G.K. / Petsko, G.A. / Ringe, D. #1: ![]() Title: Isotopic Exchange Plus Substrate and Inhibition Kinetics of D-Xylose Isomerase Do not Support a Proton-Transfer Mechanism Authors: Allen, K.N. / Lavie, A. / Farber, G.K. / Glasfeld, A. / Petsko, G.A. / Ringe, D. #2: ![]() Title: X-Ray Crystallographic Structures of D-Xylose Isomerase-Substrate Complexes Position the Substrate and Provide Evidence for Metal Movement During Catalysis Authors: Lavie, A. / Allen, K.N. / Petsko, G.A. / Ringe, D. | ||||||
History |
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Remark 700 | SHEET THE SHEETS PRESENTED AS *SA1*, *SA2*, *SB1*, AND *SB2* ON SHEET RECORDS BELOW ARE ACTUALLY ...SHEET THE SHEETS PRESENTED AS *SA1*, *SA2*, *SB1*, AND *SB2* ON SHEET RECORDS BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS. THESE ARE REPRESENTED AS NINE-STRANDED SHEETS IN WHICH THE FIRST AND LAST STRANDS OF EACH SHEET ARE IDENTICAL. THERE ARE SEVERAL BIFURCATED SHEETS IN THIS STRUCTURE. THESE ARE REPRESENTED BY TWO SHEETS WHICH HAVE ONE OR MORE IDENTICAL STRANDS. SHEETS *SA1* AND *SB1* REPRESENT ONE BIFURCATED SHEET. SHEETS *SA2* AND *SB2* REPRESENT ANOTHER BIFURCATED SHEET. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 218.3 KB | Display | ![]() |
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PDB format | ![]() | 174.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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: CIS PROLINE - PRO A 186 / 2: CIS PROLINE - PRO B 886 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.99927, 0.03829, -0.00045), Vector ![]() |
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Components
#1: Protein | ![]() Mass: 42844.914 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P15587, ![]() #2: Sugar | ![]() #3: Chemical | #4: Chemical | ![]() #5: Water | ChemComp-HOH / | ![]() Sequence details | THE SEQUENCE REPORTED HERE DISAGREES WITH THAT ORIGINALLY REPORTED (FARBER ET AL., BIOCHEMISTRY V. ...THE SEQUENCE REPORTED HERE DISAGREES WITH THAT ORIGINALLY | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.26 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS pH: 7.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 57060 / Observed criterion σ(I): 0 |
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Processing
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Refinement | Resolution: 1.8→10 Å / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 46227 / Rfactor obs: 0.197 / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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