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Open data
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Basic information
Entry | Database: PDB / ID: 1exn | ||||||
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Title | T5 5'-EXONUCLEASE | ||||||
![]() | 5'-EXONUCLEASE | ||||||
![]() | NUCLEASE / HYDROLASE / EXONUCLEASE | ||||||
Function / homology | ![]() viral replication complex / exodeoxyribonuclease (lambda-induced) / late viral transcription / DNA replication, Okazaki fragment processing / double-stranded DNA 5'-3' DNA exonuclease activity / DNA exonuclease activity / double-stranded DNA endonuclease activity / 5'-flap endonuclease activity / 5'-3' exonuclease activity / viral DNA genome replication ...viral replication complex / exodeoxyribonuclease (lambda-induced) / late viral transcription / DNA replication, Okazaki fragment processing / double-stranded DNA 5'-3' DNA exonuclease activity / DNA exonuclease activity / double-stranded DNA endonuclease activity / 5'-flap endonuclease activity / 5'-3' exonuclease activity / viral DNA genome replication / Hydrolases; Acting on ester bonds; Exodeoxyribonucleases producing 5'-phosphomonoesters / 5'-3' DNA exonuclease activity / DNA binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Ceska, T.A. / Sayers, J.R. / Stier, G. / Suck, D. | ||||||
![]() | ![]() Title: A helical arch allowing single-stranded DNA to thread through T5 5'-exonuclease. Authors: Ceska, T.A. / Sayers, J.R. / Stier, G. / Suck, D. #1: ![]() Title: Preliminary Crystallographic Studies on the D15 5' to 3' Exonuclease from Phage T5 Authors: Ceska, T.A. / Sayers, J.R. / Eckstein, F. / Suck, D. #2: ![]() Title: Properties of Overexpressed Phage T5 D15 Exonuclease. Similarities with Escherichia Coli DNA Polymerase I 5'-3' Exonuclease Authors: Sayers, J.R. / Eckstein, F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 119.2 KB | Display | ![]() |
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PDB format | ![]() | 99 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 378.4 KB | Display | ![]() |
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Full document | ![]() | 392 KB | Display | |
Data in XML | ![]() | 13.1 KB | Display | |
Data in CIF | ![]() | 20.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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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Components
#1: Protein | Mass: 33595.141 Da / Num. of mol.: 2 / Mutation: SEMET LABELLED PROTEIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P06229, exodeoxyribonuclease (lambda-induced) #2: Water | ChemComp-HOH / | Sequence details | THE N-TERMINAL MET IS REMOVED IN E. COLI. THE GENE SEQUENCE STARTING FROM RESIDUE 1 IS USED AS THE ...THE N-TERMINAL MET IS REMOVED IN E. COLI. THE GENE SEQUENCE STARTING FROM RESIDUE 1 IS USED AS THE NUMBERING SEQUENCE. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 60 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: Ceska, T.A., (1993) J.Mol.Biol., 233, 179. / pH: 7.5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 26, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Num. obs: 26463 / % possible obs: 95.2 % / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Rmerge(I) obs: 0.037 |
Reflection | *PLUS Highest resolution: 2.5 Å / Num. measured all: 67552 |
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Processing
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Refinement | Resolution: 2.5→6 Å / σ(F): 0 / Details: RESIDUE GLU A 290 IS IN POORLY DEFINED DENSITY.
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Refinement step | Cycle: LAST / Resolution: 2.5→6 Å
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Refine LS restraints |
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