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- PDB-1vz8: Ornithine Acetyltransferase (ORF6 Gene Product - Clavulanic Acid ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1vz8 | ||||||
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Title | Ornithine Acetyltransferase (ORF6 Gene Product - Clavulanic Acid Biosynthesis) from Streptomyces clavuligerus (SeMet structure) | ||||||
![]() | ORNITHINE ACETYL-TRANSFERASE | ||||||
![]() | TRANSFERASE / ORNITHINE ACETYLTRANSFERASE / CLAVULANIC ACID / N-ACETYL- ORNITHINE / N-ACETYL-GLUTAMATE / ANTIBIOTIC | ||||||
Function / homology | ![]() glutamate N-acetyltransferase / glutamate N-acetyltransferase activity / ornithine biosynthetic process / methione N-acyltransferase activity / amino-acid N-acetyltransferase / clavulanic acid biosynthetic process / acetyl-CoA:L-glutamate N-acetyltransferase activity / arginine biosynthetic process / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Elkins, J.M. / Kershaw, N.J. / Schofield, C.J. | ||||||
![]() | ![]() Title: X-Ray Crystal Structure of Ornithine Acetyltransferase from the Clavulanic Acid Biosynthesis Gene Cluster. Authors: Elkins, J.M. / Kershaw, N.J. / Schofield, C.J. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 269.5 KB | Display | ![]() |
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PDB format | ![]() | 227.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 474.1 KB | Display | ![]() |
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Full document | ![]() | 535.1 KB | Display | |
Data in XML | ![]() | 57.7 KB | Display | |
Data in CIF | ![]() | 78.9 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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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 42028.770 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: SELENOMETHIONINE-SUBSTITUTED / Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q53940, UniProt: P0DJQ5*PLUS, glutamate N-acetyltransferase #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | Compound details | THERE IS A BREAK IN THE CHAIN BETWEEN RESIDUES 180 AND 181, DUE TO THE AUTO-PROTEOLYTIC SELF- ...THERE IS A BREAK IN THE CHAIN BETWEEN RESIDUES 180 AND 181, DUE TO THE AUTO-PROTEOLYTI | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 45.4 % |
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Crystal grow | pH: 8 Details: PROTEIN AT 12MG/ML MIXED 1:1 WITH A SOLUTION OF: 1.2M (NH4)2SO4, 40MM NH4H2PO4, 0.1M TRIS PH 8.0, 6% GLYCEROL. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Aug 15, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.89 Å / Relative weight: 1 |
Reflection | Resolution: 2.75→20.5 Å / Num. obs: 40839 / % possible obs: 99.8 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.098 / Net I/σ(I): 6.9 |
Reflection shell | Resolution: 2.75→2.9 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.316 / Mean I/σ(I) obs: 2.3 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / ksol: 0.380215 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.75→23.67 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.75→2.92 Å / Rfactor Rfree error: 0.018 / Total num. of bins used: 6
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Xplor file |
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