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Yorodumi- PDB-3cla: REFINED CRYSTAL STRUCTURE OF TYPE III CHLORAMPHENICOL ACETYLTRANS... -
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-Basic information
Entry | Database: PDB / ID: 3cla | |||||||||
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Title | REFINED CRYSTAL STRUCTURE OF TYPE III CHLORAMPHENICOL ACETYLTRANSFERASE AT 1.75 ANGSTROMS RESOLUTION | |||||||||
Components | TYPE III CHLORAMPHENICOL ACETYLTRANSFERASE | |||||||||
Keywords | TRANSFERASE (ACYLTRANSFERASE) | |||||||||
Function / homology | Function and homology information chloramphenicol O-acetyltransferase activity / chloramphenicol O-acetyltransferase / response to antibiotic Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.75 Å | |||||||||
Authors | Leslie, A.G.W. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1990 Title: Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 A resolution. Authors: Leslie, A.G. #1: Journal: To be Published Title: Crystal Structure of the Asp-199-Asn Mutant of Chloramphenicol Acetyltransferase to 2.35 Angstroms Resolution. Structural Consequences of Disruption of a Buried Salt-Bridge. Authors: Gibbs, M.R. / Moody, P.C.E. / Leslie, A.G.W. #2: Journal: Biochemistry / Year: 1990 Title: Evidence for Transition-State Stabilization by Serine-148 in the Catalytic Mechanism of Chloramphenicol Acetyltransferase Authors: Lewendon, A. / Murray, I.A. / Shaw, W.V. / Gibbs, M.R. / Leslie, A.G.W. #3: Journal: Biochemistry / Year: 1988 Title: Substitutions in the Active Site of Chloramphenicol Acetyltransferase. Role of a Conserved Aspartate Authors: Lewendon, A. / Murray, I.A. / Kleanthous, C. / Cullis, P.M. / Shaw, W.V. #4: Journal: Proc.Natl.Acad.Sci.USA / Year: 1988 Title: Structure of Chloramphenicol Acetyltransferase at 1.75-Angstroms Resolution Authors: Leslie, A.G.W. / Moody, P.C.E. / Shaw, W.V. #5: Journal: J.Mol.Biol. / Year: 1986 Title: Crystallization of a Type III Chloramphenicol Acetyl Transferase Authors: Leslie, A.G.W. / Liddell, J.M. / Shaw, W.V. | |||||||||
History |
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Remark 700 | SHEET SHEET 1 ACTUALLY HAS SEVEN STRANDS. RESIDUES 157 - 162 FORM AN EXTENSION TO THE SIX STRANDED ...SHEET SHEET 1 ACTUALLY HAS SEVEN STRANDS. RESIDUES 157 - 162 FORM AN EXTENSION TO THE SIX STRANDED BETA-SHEET OF AN ADJACENT SHEET WHICH SPANS THE SUBUNIT INTERFACE. THE FINAL STRAND, SER 157 - VAL 162, IS IN AN ADJACENT (THREE-FOLD RELATED) SUBUNIT OF THE TRIMER. N OF ASN 159 IS HYDROGEN BONDED TO O OF SER 34. THERE IS A WIDE BETA-BULGE INVOLVING RESIDUES LYS 177, TYR 178, AND LEU 187. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3cla.cif.gz | 62.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3cla.ent.gz | 44.8 KB | Display | PDB format |
PDBx/mmJSON format | 3cla.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3cla_validation.pdf.gz | 434.8 KB | Display | wwPDB validaton report |
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Full document | 3cla_full_validation.pdf.gz | 440.5 KB | Display | |
Data in XML | 3cla_validation.xml.gz | 6.6 KB | Display | |
Data in CIF | 3cla_validation.cif.gz | 10.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cl/3cla ftp://data.pdbj.org/pub/pdb/validation_reports/cl/3cla | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Atom site foot note | 1: THERE IS A WIDE BETA-BULGE INVOLVING RESIDUES LYS 177, TYR 178, AND LEU 187. 2: RESIDUES 157 - 162 FORM AN EXTENSION TO THE SIX STRANDED BETA-SHEET OF AN ADJACENT SHEET WHICH SPANS THE SUBUNIT INTERFACE. | ||||||||||||||||||
Components on special symmetry positions |
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-Components
#1: Protein | Mass: 25021.494 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) References: UniProt: P00484, chloramphenicol O-acetyltransferase | ||||||
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#2: Chemical | #3: Chemical | ChemComp-CLM / | #4: Water | ChemComp-HOH / | Sequence details | THE NUMBERING SCHEME ADOPTED IS BASED ON THE ALIGNMENT OF A NUMBER OF CAT SEQUENCES. FOR THE TYPE ...THE NUMBERING SCHEME ADOPTED IS BASED ON THE ALIGNMENT OF A NUMBER OF CAT SEQUENCES. FOR THE TYPE III ENZYME WHOSE COORDINATE | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.28 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6.3 / Method: microdialysis | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.75 Å / Rmerge(I) obs: 0.058 |
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-Processing
Software | Name: DERIV / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.75→6 Å / Rfactor Rwork: 0.157 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→6 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.75 Å / Lowest resolution: 6 Å / Num. reflection obs: 27300 / Rfactor obs: 0.157 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 3.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: o_angle_d / Dev ideal: 3 |