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- PDB-1xyc: X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xyc | ||||||
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Title | X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS | ||||||
![]() | XYLOSE ISOMERASE | ||||||
![]() | ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) | ||||||
Function / homology | ![]() xylose isomerase / D-xylose metabolic process / xylose isomerase activity / magnesium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Lavie, A. / Allen, K.N. / Petsko, G.A. / Ringe, D. | ||||||
![]() | ![]() 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. #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: 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 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. | ||||||
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 | ![]() | 174 KB | Display | ![]() |
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PDB format | ![]() | 135.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 393.7 KB | Display | ![]() |
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Full document | ![]() | 409.2 KB | Display | |
Data in XML | ![]() | 17.9 KB | Display | |
Data in CIF | ![]() | 29.5 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: CIS PROLINE - PRO A 186 / 2: CIS PROLINE - PRO B 686 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.99927, 0.03829, -0.00045), Vector: |
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Components
#1: Protein | Mass: 42844.848 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P15587, xylose isomerase #2: Sugar | #3: Chemical | ChemComp-MG / #4: Water | ChemComp-HOH / | Nonpolymer details | THERE IS ONE SUGAR MOLECULE IN THE OPEN FORM BOUND TO THE ENZYME IN EACH ACTIVE SITE. THE SUGAR WAS ...THERE IS ONE SUGAR MOLECULE IN THE OPEN FORM BOUND TO THE ENZYME IN EACH ACTIVE SITE. THE SUGAR WAS MODELED AS 3-O-METHYLFRUC | 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: 2.39 Å3/Da / Density % sol: 48.64 % | ||||||||||||||||||||||||||||||||||||
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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: 2.19 Å / Lowest resolution: 9999 Å / Num. obs: 42123 / % possible obs: 98 % / Num. measured all: 417620 / Rmerge(I) obs: 0.043 |
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Processing
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Refinement | Resolution: 2.19→10 Å / Rfactor Rwork: 0.159 / Rfactor obs: 0.159 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.19→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.159 / Rfactor Rwork: 0.159 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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