+Open data
-Basic information
Entry | Database: PDB / ID: 3cna | ||||||
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Title | STRUCTURE OF CONCANAVALIN A AT 2.4 ANGSTROMS RESOLUTION | ||||||
Components | CONCANAVALIN A | ||||||
Keywords | LECTIN (AGGLUTININ) | ||||||
Function / homology | Function and homology information regulation of defense response to virus / D-mannose binding / defense response / metal ion binding Similarity search - Function | ||||||
Biological species | Canavalia ensiformis (jack bean) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | ||||||
Authors | Hardman, K.D. / Ainsworth, C.F. | ||||||
Citation | Journal: Biochemistry / Year: 1972 Title: Structure of concanavalin A at 2.4-A resolution. Authors: Hardman, K.D. / Ainsworth, C.F. #1: Journal: Biochemistry / Year: 1976 Title: Structure of the Concanavalin A-Methyl-Alpha-D-Mannopyranoside Complex at 6.0 Angstroms Resolution Authors: Hardman, K.D. / Ainsworth, C.F. #2: Journal: Biochemistry / Year: 1973 Title: Binding of Nonpolar Molecules by Crystalline Concanavalin A Authors: Hardman, K.D. / Ainsworth, C.F. #3: Journal: Adv.Exp.Med.Biol. / Year: 1973 Title: Crystallography of a Metal-Containing Protein, Concanavalin A Authors: Hardman, K.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3cna.cif.gz | 51.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3cna.ent.gz | 36.9 KB | Display | PDB format |
PDBx/mmJSON format | 3cna.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3cna_validation.pdf.gz | 368.7 KB | Display | wwPDB validaton report |
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Full document | 3cna_full_validation.pdf.gz | 422.8 KB | Display | |
Data in XML | 3cna_validation.xml.gz | 14.3 KB | Display | |
Data in CIF | 3cna_validation.cif.gz | 19.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cn/3cna ftp://data.pdbj.org/pub/pdb/validation_reports/cn/3cna | 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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Unit cell |
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Atom site foot note | 1: THESE RESIDUES (187-190) ARE ORDERED IN THIS COORDINATE SET TO REFLECT BEST AGREEMENT WITH THE ELECTRON DENSITY. THIS REGION WAS AMBIGUOUS IN THE CHEMICAL DETERMINATION OF THE PRIMARY STRUCTURE. |
-Components
#1: Protein | Mass: 25596.299 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Canavalia ensiformis (jack bean) / References: UniProt: P02866 |
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#2: Chemical | ChemComp-MN / |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.56 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 22 ℃ / Method: batch methodDetails: referred to 'Hardman, K.D.', (1971) Proc.Nat.Acad.Sci.U.S., 64. 1393-1397 | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 6 Å / Num. obs: 10000 / Observed criterion σ(I): 2 / Num. measured all: 90000 |
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-Processing
Refinement | Highest resolution: 2.4 Å | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 2.4 Å
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Refinement | *PLUS Highest resolution: 2.4 Å | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |