+Open data
-Basic information
Entry | Database: PDB / ID: 1ceg | ||||||
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Title | CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE | ||||||
Components | D-ALANYL-D-ALANINE CARBOXYPEPTIDASE TRANSPEPTIDASE | ||||||
Keywords | HYDROLASE-TRANSPEPTIDASE / D-AMINO ACID PEPTIDASE / PENICILLIN TARGET | ||||||
Function / homology | Function and homology information serine-type D-Ala-D-Ala carboxypeptidase / serine-type D-Ala-D-Ala carboxypeptidase activity / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | Streptomyces sp. (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Knox, J.R. / Kuzin, A.P. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases. Authors: Kuzin, A.P. / Liu, H. / Kelly, J.A. / Knox, J.R. #1: Journal: J.Mol.Biol. / Year: 1995 Title: The Refined Crystallographic Structure of a Dd-Peptidase Penicillin-Target Enzyme at 1.6 A Resolution Authors: Kelly, J.A. / Kuzin, A.P. #2: Journal: J.Mol.Biol. / Year: 1989 Title: Crystallographic Mapping of Beta-Lactams Bound to a D-Alanyl-D-Alanine Peptidase Target Enzyme Authors: Kelly, J.A. / Knox, J.R. / Zhao, H. / Frere, J.M. / Ghaysen, J.M. #3: Journal: Science / Year: 1986 Title: On the Origin of Bacterial Resistance to Penicillin: Comparison of a Beta-Lactamase and a Penicillin Target Authors: Kelly, J.A. / Dideberg, O. / Charlier, P. / Wery, J.P. / Libert, M. / Moews, P.C. / Knox, J.R. / Duez, C. / Fraipont, C. / Joris, B. / al., et #4: Journal: J.Biol.Chem. / Year: 1985 Title: 2.8-A Structure of Penicillin-Sensitive D-Alanyl Carboxypeptidase-Transpeptidase from Streptomyces R61 and Complexes with Beta-Lactams Authors: Kelly, J.A. / Knox, J.R. / Moews, P.C. / Hite, G.J. / Bartolone, J.B. / Zhao, H. / Joris, B. / Frere, J.M. / Ghuysen, J.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ceg.cif.gz | 83.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ceg.ent.gz | 61.8 KB | Display | PDB format |
PDBx/mmJSON format | 1ceg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ceg_validation.pdf.gz | 444.3 KB | Display | wwPDB validaton report |
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Full document | 1ceg_full_validation.pdf.gz | 446.6 KB | Display | |
Data in XML | 1ceg_validation.xml.gz | 8.4 KB | Display | |
Data in CIF | 1ceg_validation.cif.gz | 13.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ce/1ceg ftp://data.pdbj.org/pub/pdb/validation_reports/ce/1ceg | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 37422.574 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Streptomyces sp. (bacteria) / Strain: R61 References: UniProt: P15555, serine-type D-Ala-D-Ala carboxypeptidase |
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#2: Chemical | ChemComp-CEP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.39 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6.8 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Mar 4, 1989 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 28901 / % possible obs: 72 % / Observed criterion σ(I): 0 / Redundancy: 1.6 % / Rmerge(I) obs: 0.051 |
Reflection | *PLUS Highest resolution: 1.76 Å / Num. measured all: 49740 |
-Processing
Software |
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Refinement | Resolution: 1.8→20 Å / σ(F): 3 Details: SEE STRUCTURE OF NATIVE FOR MULTIPLE CONFORMATIONS (J.A.KELLY AND A.P.KUZIN JOURNAL OF MOLECULAR BIOLOGY, 1995, SUBMITTED).
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Displacement parameters | Biso mean: 9.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.22 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.9 |