+Open data
-Basic information
Entry | Database: PDB / ID: 1ffq | |||||||||
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Title | CRYSTAL STRUCTURE OF CHITINASE A COMPLEXED WITH ALLOSAMIDIN | |||||||||
Components | CHITINASE A | |||||||||
Keywords | HYDROLASE / glycosyl hydrolase / enzyme-inhibitor complex | |||||||||
Function / homology | Function and homology information chitinase / chitinase activity / chitin catabolic process / chitin binding / polysaccharide catabolic process / extracellular region Similarity search - Function | |||||||||
Biological species | Serratia marcescens (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | |||||||||
Authors | Papanikolau, Y. / Tavlas, G. / Vorgias, C.E. / Petratos, K. | |||||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2003 Title: De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin. Authors: Papanikolau, Y. / Tavlas, G. / Vorgias, C.E. / Petratos, K. #1: Journal: BIOCHEMISTRY / Year: 2001 Title: HIGH RESOLUTION STRUCTURAL ANALYSES OF MUTANT CHITINASE A COMPLEXES WITH SUBSTRATES PROVIDE NEW INSIGHT INTO THE MECHANISM OF CATALYSIS Authors: Papanikolau, Y. / Prag, G. / Tavlas, G. / Vorgias, C.E. / Oppenheim, A.B. / Petratos, K. #2: Journal: Structure / Year: 1994 Title: Crystal structure of a bacterial chitinase at 2.3 Angstrom resolution Authors: Perrakis, A. / Tews, I. / Dauter, Z. / Oppenheim, A.B. / Chet, I. / Wilson, K.S. / Vorgias, C.E. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ffq.cif.gz | 136.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ffq.ent.gz | 101.2 KB | Display | PDB format |
PDBx/mmJSON format | 1ffq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ffq_validation.pdf.gz | 794.7 KB | Display | wwPDB validaton report |
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Full document | 1ffq_full_validation.pdf.gz | 799.9 KB | Display | |
Data in XML | 1ffq_validation.xml.gz | 28.5 KB | Display | |
Data in CIF | 1ffq_validation.cif.gz | 44.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ff/1ffq ftp://data.pdbj.org/pub/pdb/validation_reports/ff/1ffq | HTTPS FTP |
-Related structure data
Related structure data | 1edqSC S: Starting model for refinement C: citing same article (ref.) |
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Similar 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: 58639.590 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Serratia marcescens (bacteria) / Strain: 2170 / Plasmid: PBR322 / Production host: Escherichia coli (E. coli) References: GenBank: AB015996, UniProt: P07254*PLUS, chitinase |
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#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-allopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-allopyranose Source method: isolated from a genetically manipulated source |
#3: Chemical | ChemComp-AMI / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.3 Å3/Da / Density % sol: 63 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.2 Details: 0.75 M Citrate-Na pH 7.2, 20% (v/v) Methanol, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 14, 1999 / Details: PAIR OF NICKEL MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→10 Å / Num. all: 60767 / Num. obs: 60767 / % possible obs: 98.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Biso Wilson estimate: 24.6 Å2 / Rmerge(I) obs: 0.056 / Net I/σ(I): 22.6 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.249 / Mean I/σ(I) obs: 4.1 / Num. unique all: 5852 / % possible all: 96.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1EDQ Resolution: 1.9→10 Å / SU B: 2.82 / SU ML: 0.08 / σ(F): 0 / σ(I): 0 / ESU R: 0.13 / ESU R Free: 0.13 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 26.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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