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- PDB-1cax: DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECUL... -

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Basic information

Entry
Database: PDB / ID: 1cax
TitleDETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT
Components(CANAVALIN) x 2
KeywordsSEED STORAGE PROTEIN
Function / homology
Function and homology information


nutrient reservoir activity / protein-containing complex / identical protein binding
Similarity search - Function
: / Cupin / Cupin 1 / Cupin / RmlC-like cupin domain superfamily / Jelly Rolls / RmlC-like jelly roll fold / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesCanavalia ensiformis (jack bean)
MethodX-RAY DIFFRACTION / Resolution: 2.6 Å
AuthorsKo, T-P. / Ng, J.D. / Day, J. / Greenwood, A. / McPherson, A.
Citation
Journal: Acta Crystallogr.,Sect.D / Year: 1993
Title: Determination of three crystal structures of canavalin by molecular replacement.
Authors: Ko, T.P. / Ng, J.D. / Greenwood, A. / McPherson, A.
#1: Journal: Plant Physiol. / Year: 1993
Title: The Three-Dimensional Structure of Canavalin from Jack Bean (Canavalia Ensiformis)
Authors: Ko, T-P. / Ng, J.D. / Day, J. / McPherson, A.
History
DepositionJun 10, 1993Processing site: BNL
Revision 1.0Oct 31, 1993Provider: 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CANAVALIN
B: CANAVALIN
C: CANAVALIN
D: CANAVALIN
E: CANAVALIN
F: CANAVALIN


Theoretical massNumber of molelcules
Total (without water)124,8296
Polymers124,8296
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area26930 Å2
ΔGint-154 kcal/mol
Surface area40650 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.500, 150.300, 133.400
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein CANAVALIN


Mass: 20968.727 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Canavalia ensiformis (jack bean) / References: UniProt: P50477
#2: Protein CANAVALIN


Mass: 20641.021 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Canavalia ensiformis (jack bean) / References: UniProt: P50477

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.74 Å3/Da / Density % sol: 55.1 %
Crystal grow
*PLUS
pH: 6.8 / Method: unknown
Components of the solutions
*PLUS
Conc.: 1.0 %(w/v) / Chemical formula: NaCl

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Highest resolution: 2.6 Å / Num. obs: 37938 / Num. measured all: 140046 / Rmerge(I) obs: 0.0548
Reflection shell
*PLUS
Highest resolution: 2.6 Å / Lowest resolution: 2.8 Å / Num. unique obs: 7058 / Num. measured obs: 18236 / Rmerge(I) obs: 0.1744

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Processing

SoftwareName: TNT / Classification: refinement
RefinementResolution: 2.6→8 Å / σ(I): 3 /
RfactorNum. reflection
obs0.175 28844
Refinement stepCycle: LAST / Resolution: 2.6→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8790 0 0 0 8790
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONt_bond_d0.02
X-RAY DIFFRACTIONt_angle_deg2.98
X-RAY DIFFRACTIONt_dihedral_angle_d
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes
X-RAY DIFFRACTIONt_it
X-RAY DIFFRACTIONt_nbd
Refinement
*PLUS
Highest resolution: 2.6 Å / Rfactor obs: 0.175 / Rfactor Rwork: 0.185
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONt_angle_deg2.987
X-RAY DIFFRACTIONt_dihedral_angle_d
X-RAY DIFFRACTIONt_dihedral_angle_deg24.604
X-RAY DIFFRACTIONt_plane_restr0.02

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