[English] 日本語
Yorodumi- PDB-1aor: STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE F... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1aor | ||||||
---|---|---|---|---|---|---|---|
Title | STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE | ||||||
Components | ALDEHYDE FERREDOXIN OXIDOREDUCTASE | ||||||
Keywords | OXIDOREDUCTASE | ||||||
Function / homology | Function and homology information aldehyde ferredoxin oxidoreductase activity / aldehyde ferredoxin oxidoreductase / 4 iron, 4 sulfur cluster binding / electron transfer activity / metal ion binding Similarity search - Function | ||||||
Biological species | Pyrococcus furiosus (archaea) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Chan, M.K. / Mukund, S. / Kletzin, A. / Adams, M.W.W. / Rees, D.C. | ||||||
Citation | Journal: Science / Year: 1995 Title: Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Authors: Chan, M.K. / Mukund, S. / Kletzin, A. / Adams, M.W. / Rees, D.C. #1: Journal: To be Published Title: Molecular Characterization of the Genes Encoding Two Tungsten-Containing Enzymes from Hyperthermophilic Archaea: Aldehyde Ferredoxin Oxidoreductase from Pyrococcus Furiosus and Formaldehyde ...Title: Molecular Characterization of the Genes Encoding Two Tungsten-Containing Enzymes from Hyperthermophilic Archaea: Aldehyde Ferredoxin Oxidoreductase from Pyrococcus Furiosus and Formaldehyde Ferredoxin Oxidoreductase from Thermococcus Litoralis Authors: Kletzin, A. / Mukund, S. / Kelley-Crouse, T.L. / Chan, M.K. / Rees, D.C. / Adams, M.W.W. | ||||||
History |
| ||||||
Remark 700 | SHEET HELIX AND SHEET ENTRIES HAVE BEEN AUTOMATICALLY GENERATED BY THE PDB USING A PROGRAM BASED ON ...SHEET HELIX AND SHEET ENTRIES HAVE BEEN AUTOMATICALLY GENERATED BY THE PDB USING A PROGRAM BASED ON DSSP OF W. KABSCH AND C. SANDER |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1aor.cif.gz | 252.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1aor.ent.gz | 201.5 KB | Display | PDB format |
PDBx/mmJSON format | 1aor.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1aor_validation.pdf.gz | 539.2 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1aor_full_validation.pdf.gz | 555.9 KB | Display | |
Data in XML | 1aor_validation.xml.gz | 25.4 KB | Display | |
Data in CIF | 1aor_validation.cif.gz | 40.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ao/1aor ftp://data.pdbj.org/pub/pdb/validation_reports/ao/1aor | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: CIS PROLINE - PRO A 310 / 2: CIS PROLINE - PRO A 462 / 3: CIS PROLINE - PRO B 310 / 4: CIS PROLINE - PRO B 462 |
-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 66715.008 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus furiosus (archaea) / References: UniProt: Q51739 |
---|
-Non-polymers , 5 types, 386 molecules
#2: Chemical | ChemComp-FE / | ||||||
---|---|---|---|---|---|---|---|
#3: Chemical | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.62 Å3/Da / Density % sol: 53.12 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 8 / Method: capillary method | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 56373 / % possible obs: 92.4 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Highest resolution: 2.32 Å / Num. measured all: 237105 / Rmerge(I) obs: 0.049 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.3→10 Å / σ(F): 0 Details: PLEASE NOTE THAT ALL RESIDUES WERE BUILT TO FIT THE BEST POSSIBLE OBSERVED DENSITY. THOSE SIDE CHAIN ATOMS WHICH SEEMED UNRELIABLE HAD THEIR OCCUPANCIES FIXED AT 0.0.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 3 Å / Lowest resolution: 22 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |