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- PDB-1cn1: CRYSTAL STRUCTURE OF DEMETALLIZED CONCANAVALIN A. THE METAL-BINDI... -

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Basic information

Entry
Database: PDB / ID: 1cn1
TitleCRYSTAL STRUCTURE OF DEMETALLIZED CONCANAVALIN A. THE METAL-BINDING REGION
ComponentsCONCANAVALIN A
KeywordsLECTIN (AGGLUTININ)
Function / homology
Function and homology information


regulation of defense response to virus / D-mannose binding / defense response / metal ion binding
Similarity search - Function
Legume lectin / Legume lectin, alpha chain, conserved site / Legume lectins alpha-chain signature. / Legume lectins beta-chain signature. / Legume lectin domain / Legume lectin, beta chain, Mn/Ca-binding site / Legume lectin domain / : / Jelly Rolls - #200 / Concanavalin A-like lectin/glucanase domain superfamily ...Legume lectin / Legume lectin, alpha chain, conserved site / Legume lectins alpha-chain signature. / Legume lectins beta-chain signature. / Legume lectin domain / Legume lectin, beta chain, Mn/Ca-binding site / Legume lectin domain / : / Jelly Rolls - #200 / Concanavalin A-like lectin/glucanase domain superfamily / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesCanavalia ensiformis (jack bean)
MethodX-RAY DIFFRACTION / Resolution: 3.2 Å
AuthorsShoham, M. / Yonath, A. / Sussman, J.L. / Moult, J. / Traub, W. / Gilboa(Kalb), A.J.
CitationJournal: J.Mol.Biol. / Year: 1979
Title: Crystal structure of demetallized concanavalin A: the metal-binding region.
Authors: Shoham, M. / Yonath, A. / Sussman, J.L. / Moult, J. / Traub, W. / Kalb, A.J.
History
DepositionDec 21, 1981Processing site: BNL
Revision 1.0Mar 4, 1982Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 7, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CONCANAVALIN A
B: CONCANAVALIN A


Theoretical massNumber of molelcules
Total (without water)51,1932
Polymers51,1932
Non-polymers00
Water00
1
A: CONCANAVALIN A
B: CONCANAVALIN A

A: CONCANAVALIN A
B: CONCANAVALIN A


Theoretical massNumber of molelcules
Total (without water)102,3854
Polymers102,3854
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Unit cell
Length a, b, c (Å)84.300, 91.200, 61.100
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21221

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Components

#1: Protein CONCANAVALIN A


Mass: 25596.299 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Canavalia ensiformis (jack bean) / References: UniProt: P02866

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.29 Å3/Da / Density % sol: 46.36 %
Crystal grow
*PLUS
Method: other
Details: Jack, A., (1971) J. Mol. Biol., 58, 389., Kalb, A.J., (1968) Biochem. J., 109, 669.

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1

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Processing

RefinementHighest resolution: 3.2 Å
Details: TWO GROUP TEMPERATURE FACTORS ARE ASSIGNED TO RESIDUES, ONE FOR BACKBONE ATOMS AND THE OTHER FOR SIDE CHAIN ATOMS.
Refinement stepCycle: LAST / Highest resolution: 3.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3612 0 0 0 3612
Refinement
*PLUS
Lowest resolution: 10 Å / Num. reflection obs: 7801 / Rfactor obs: 0.256
Solvent computation
*PLUS
Displacement parameters
*PLUS

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