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- PDB-1ucc: Crystal structure of the Ribonuclease MC1 from bitter gourd seeds... -

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Basic information

Entry
Database: PDB / ID: 1ucc
TitleCrystal structure of the Ribonuclease MC1 from bitter gourd seeds complexed with 3'-UMP.
ComponentsRibonuclease MC
KeywordsHYDROLASE / alpha plus beta
Function / homology
Function and homology information


ribonuclease T2 / ribonuclease T2 activity / RNA catabolic process / RNA binding / extracellular region
Similarity search - Function
Ribonuclease T2, eukaryotic / Ribonuclease T2, His active site 1 / Ribonuclease T2 family histidine active site 1. / Ribonuclease T2-like / Ribonuclease T2 family / Ribonuclease Rh; Chain A / Ribonuclease T2-like / Ribonuclease T2, His active site 2 / Ribonuclease T2 family histidine active site 2. / Ribonuclease T2-like superfamily ...Ribonuclease T2, eukaryotic / Ribonuclease T2, His active site 1 / Ribonuclease T2 family histidine active site 1. / Ribonuclease T2-like / Ribonuclease T2 family / Ribonuclease Rh; Chain A / Ribonuclease T2-like / Ribonuclease T2, His active site 2 / Ribonuclease T2 family histidine active site 2. / Ribonuclease T2-like superfamily / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
3'-URIDINEMONOPHOSPHATE / Ribonuclease MC
Similarity search - Component
Biological speciesMomordica charantia (bitter melon)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.77 Å
AuthorsSuzuki, A. / Yao, M. / Tanaka, I. / Numata, T. / Kikukawa, S. / Yamasaki, N. / Kimura, M.
CitationJournal: Biochem.Biophys.Res.Commun. / Year: 2000
Title: Crystal structures of the ribonuclease MC1 from bitter gourd seeds, complexed with 2'-UMP or 3'-UMP, reveal structural basis for uridine specificity
Authors: Suzuki, A. / Yao, M. / Tanaka, I. / Numata, T. / Kikukawa, S. / Yamasaki, N. / Kimura, M.
History
DepositionApr 10, 2003Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 29, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 25, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Ribonuclease MC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,5512
Polymers21,2271
Non-polymers3241
Water1,69394
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)38.80, 67.63, 75.54
Angle α, β, γ (deg.)90, 90, 90
Int Tables number19
Space group name H-MP212121
DetailsThe bilogical unit is a monomer in the asymmetric unit.

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Components

#1: Protein Ribonuclease MC / Ribonuclease MC1


Mass: 21227.010 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Momordica charantia (bitter melon) / Tissue: seed / References: UniProt: P23540, EC: 3.1.27.1
#2: Chemical ChemComp-U3P / 3'-URIDINEMONOPHOSPHATE


Mass: 324.181 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H13N2O9P
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 94 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.33 Å3/Da / Density % sol: 47.28 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.7
Details: PEG 8000, sodium acetate, sodium cacodylate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystal grow
*PLUS
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
119 mg/mlprotein1drop
20.2 Msodium acetate1reservoir
30.1 Msodium cacodylate1reservoirpH6.7
421 %PEG80001reservoir
510 mM3'-UMP1reservoir

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Data collection

DiffractionMean temperature: 298 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL44B2 / Wavelength: 0.7 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Oct 12, 1999 / Details: mirrors
RadiationMonochromator: Mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.7 Å / Relative weight: 1
ReflectionResolution: 1.77→19.49 Å / Num. all: 28892 / Num. obs: 18370 / % possible obs: 92.7 % / Observed criterion σ(I): 3 / Redundancy: 4.3 % / Biso Wilson estimate: 15.729 Å2 / Rmerge(I) obs: 0.086 / Rsym value: 0.076 / Net I/σ(I): 6.6
Reflection shellResolution: 1.77→1.87 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.369 / Mean I/σ(I) obs: 2 / Num. unique all: 2684 / Rsym value: 0.33 / % possible all: 94.3
Reflection
*PLUS
Lowest resolution: 19.4 Å / Num. measured all: 427770
Reflection shell
*PLUS
% possible obs: 94.3 % / Rmerge(I) obs: 0.37

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing
CNS1refinement
CCP4(SCALA)data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1BK7

1bk7


Resolution: 1.77→10 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.214 935 -random
Rwork0.181 ---
all-18243 --
obs-17308 91.8 %-
Displacement parametersBiso mean: 18.7 Å2
Baniso -1Baniso -2Baniso -3
1-1.188 Å20 Å20 Å2
2---3.587 Å20 Å2
3---2.399 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.1 Å0.18 Å
Luzzati d res low-5 Å
Luzzati sigma a0.1 Å0.22 Å
Refinement stepCycle: LAST / Resolution: 1.77→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1496 0 21 94 1611
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_angle_deg1.687
X-RAY DIFFRACTIONc_bond_d0.005
X-RAY DIFFRACTIONc_dihedral_angle_d23.09
X-RAY DIFFRACTIONc_improper_angle_d1.031
LS refinement shellResolution: 1.77→1.83 Å
RfactorNum. reflection% reflection
Rfree0.2421 92 -
Rwork0.2133 --
obs-1816 93.75 %
Refinement
*PLUS
Num. reflection obs: 18243 / % reflection Rfree: 5 %
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_angle_deg1.686
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg23.09
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg1.031

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