[English] 日本語
Yorodumi
- PDB-9bad: Crystal structure of Bacillus subtilis 168 L-asparaginase II with... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9bad
TitleCrystal structure of Bacillus subtilis 168 L-asparaginase II with antileukemic activity
ComponentsL-asparaginase 2
KeywordsANTITUMOR PROTEIN / Enzyme / Leukemia / Recombinant
Function / homology
Function and homology information


L-asparagine catabolic process / asparaginase / asparaginase activity / periplasmic space
Similarity search - Function
L-asparaginase, type II / Asparaginase/glutaminase, active site 1 / Asparaginase / glutaminase active site signature 1. / L-asparaginase, C-terminal / Asparaginase/glutaminase, active site 2 / Asparaginase/glutaminase, C-terminal / Glutaminase/Asparaginase C-terminal domain / Asparaginase / glutaminase active site signature 2. / Asparaginase / Asparaginase/glutaminase-like ...L-asparaginase, type II / Asparaginase/glutaminase, active site 1 / Asparaginase / glutaminase active site signature 1. / L-asparaginase, C-terminal / Asparaginase/glutaminase, active site 2 / Asparaginase/glutaminase, C-terminal / Glutaminase/Asparaginase C-terminal domain / Asparaginase / glutaminase active site signature 2. / Asparaginase / Asparaginase/glutaminase-like / L-asparaginase, N-terminal / Asparaginase/glutaminase-like superfamily / L-asparaginase, N-terminal domain superfamily / Asparaginase, N-terminal / Asparaginase / glutaminase domain profile.
Similarity search - Domain/homology
Biological speciesBacillus subtilis subsp. subtilis str. 168 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.3 Å
AuthorsGomes, J.G.S. / Rocha, B.A.M. / Brandao, L.C. / Furtado, G.P. / Pontes, L.Q. / Lourenzoni, M.R.
Funding support Brazil, 1items
OrganizationGrant numberCountry
Brazilian National Council for Scientific and Technological Development (CNPq)313837/2020-1 Brazil
CitationJournal: To Be Published
Title: Biochemical and Structural characterization of Bacillus subtilis 168 L-asparaginase II
Authors: Brandao, L.C. / Gomes, J.G.S. / Pinheiro, D.P. / Pontes, L.Q. / Rocha, B.A.M. / Lourenzoni, M.R. / Furtado, G.P.
History
DepositionApr 3, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 8, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: L-asparaginase 2
B: L-asparaginase 2
C: L-asparaginase 2
D: L-asparaginase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)160,0017
Polymers159,8634
Non-polymers1383
Water20,2491124
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16100 Å2
ΔGint-45 kcal/mol
Surface area40250 Å2
MethodPISA
Unit cell
Length a, b, c (Å)102.234, 104.486, 123.055
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein
L-asparaginase 2 / L-ASNase 2 / L-asparagine amidohydrolase 2


Mass: 39965.637 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: Bacillus Genetic Stock Center
Source: (gene. exp.) Bacillus subtilis subsp. subtilis str. 168 (bacteria)
Strain: 168 / Gene: ansZ, yccC, BSU02690 / Plasmid: pET-28a(+) / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / Variant (production host): Rosetta / References: UniProt: O34482, asparaginase
#2: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1124 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.06 Å3/Da / Density % sol: 40.17 % / Description: Cubic to rectangular crystals
Crystal growTemperature: 285.15 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: PEG 400 25 %, HEPES 0.1 M, NaCl 0.1 M

-
Data collection

DiffractionMean temperature: 100 K / Ambient temp details: Liquid nitrogen jet / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: LNLS SIRIUS / Beamline: MANACA / Wavelength: 0.97718 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Dec 3, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97718 Å / Relative weight: 1
ReflectionResolution: 1.3→48.135 Å / Num. obs: 321574 / % possible obs: 100 % / Redundancy: 1.9 % / CC1/2: 0.99 / Net I/av σ(I): 11.3 / Net I/σ(I): 1.5
Reflection shellResolution: 1.3→1.32 Å / Redundancy: 2 % / Mean I/σ(I) obs: 1.2 / Num. unique obs: 31082 / CC1/2: 0.54 / % possible all: 100

-
Processing

Software
NameVersionClassification
REFMAC5.8.0419refinement
XDS1.08data reduction
pointless1.12.12data scaling
MOLREP11.9.02phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.3→48.13 Å / Cor.coef. Fo:Fc: 0.98 / Cor.coef. Fo:Fc free: 0.973 / SU B: 1.618 / SU ML: 0.029 / Cross valid method: THROUGHOUT / ESU R: 0.041 / ESU R Free: 0.041 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.16433 16178 5 %RANDOM
Rwork0.13552 ---
obs0.13695 305395 99.99 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 16.358 Å2
Baniso -1Baniso -2Baniso -3
1-0.45 Å2-0 Å20 Å2
2---0.45 Å2-0 Å2
3---0.01 Å2
Refinement stepCycle: 1 / Resolution: 1.3→48.13 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9427 0 8 1124 10559
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0129724
X-RAY DIFFRACTIONr_bond_other_d0.0010.0169386
X-RAY DIFFRACTIONr_angle_refined_deg1.6781.6513230
X-RAY DIFFRACTIONr_angle_other_deg0.5891.57421663
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.29651296
X-RAY DIFFRACTIONr_dihedral_angle_2_deg6.308536
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.803101674
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0940.21594
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0211466
X-RAY DIFFRACTIONr_gen_planes_other0.0020.022018
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it4.9021.5515139
X-RAY DIFFRACTIONr_mcbond_other4.9021.5515139
X-RAY DIFFRACTIONr_mcangle_it6.9332.7896450
X-RAY DIFFRACTIONr_mcangle_other6.9322.7896451
X-RAY DIFFRACTIONr_scbond_it7.6051.874585
X-RAY DIFFRACTIONr_scbond_other7.6031.874585
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other10.7973.2926781
X-RAY DIFFRACTIONr_long_range_B_refined14.59316.710818
X-RAY DIFFRACTIONr_long_range_B_other13.40915.8710545
X-RAY DIFFRACTIONr_rigid_bond_restr4.06319110
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.3→1.334 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.274 1203 -
Rwork0.253 22394 -
obs--99.99 %

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more