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Basic information

Entry
Database: PDB / ID: 6azs
TitleStructural and biochemical characterization of a non-canonical biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841
ComponentsPutative amidase
KeywordsHYDROLASE/HYDROLASE INHIBITOR / s-triazine / xenobiotic / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homologybiuret amidohydrolase / : / Isochorismatase-like / Isochorismatase-like superfamily / Isochorismatase family / hydrolase activity / N-formyl-D-aspartic acid / DI(HYDROXYETHYL)ETHER / Biuret amidohydrolase
Function and homology information
Biological speciesRhizobium leguminosarum bv. viciae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.59 Å
AuthorsPeat, T.S. / Esquirol, L. / Newman, J. / Scott, C.
CitationJournal: PLoS ONE / Year: 2018
Title: Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841.
Authors: Esquirol, L. / Peat, T.S. / Wilding, M. / Lucent, D. / French, N.G. / Hartley, C.J. / Newman, J. / Scott, C.
History
DepositionSep 11, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 21, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 4, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / refine_hist / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine_hist.d_res_low / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.2Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Putative amidase
B: Putative amidase
C: Putative amidase
D: Putative amidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)115,94715
Polymers114,3704
Non-polymers1,57711
Water15,997888
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15100 Å2
ΔGint-2 kcal/mol
Surface area28160 Å2
2
A: Putative amidase
D: Putative amidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,0919
Polymers57,1852
Non-polymers9057
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4830 Å2
ΔGint-12 kcal/mol
Surface area16930 Å2
MethodPISA
3
B: Putative amidase
C: Putative amidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,8576
Polymers57,1852
Non-polymers6724
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4760 Å2
ΔGint-5 kcal/mol
Surface area16740 Å2
MethodPISA
Unit cell
Length a, b, c (Å)62.067, 122.244, 136.061
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP22121
Components on special symmetry positions
IDModelComponents
11D-474-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14B
24C
15B
25D
16C
26D

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASNASNLEULEUAA8 - 23228 - 252
21ASNASNLEULEUBB8 - 23228 - 252
12VALVALLEULEUAA5 - 23225 - 252
22VALVALLEULEUCC5 - 23225 - 252
13ASNASNLEULEUAA8 - 23228 - 252
23ASNASNLEULEUDD8 - 23228 - 252
14ASNASNLEULEUBB8 - 23228 - 252
24ASNASNLEULEUCC8 - 23228 - 252
15ASNASNPROPROBB8 - 23328 - 253
25ASNASNPROPRODD8 - 23328 - 253
16ASNASNLEULEUCC8 - 23228 - 252
26ASNASNLEULEUDD8 - 23228 - 252

NCS ensembles :
ID
1
2
3
4
5
6
DetailsTetramer as determined by gel filtration

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Putative amidase


Mass: 28592.576 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhizobium leguminosarum bv. viciae (strain 3841) (bacteria)
Strain: 3841 / Gene: pRL100352 / Plasmid: pETcc2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / Variant (production host): DE3 / References: UniProt: Q1M7F4

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Non-polymers , 6 types, 899 molecules

#2: Chemical
ChemComp-BTB / 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / BIS-TRIS BUFFER


Mass: 209.240 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C8H19NO5 / Comment: pH buffer*YM
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#5: Chemical ChemComp-C5S / N-formyl-D-aspartic acid


Mass: 161.113 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C5H7NO5
#6: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 888 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.26 Å3/Da / Density % sol: 45.49 %
Crystal growTemperature: 281 K / Method: vapor diffusion, sitting drop / pH: 6.1
Details: Sitting drops were set up with 150 nL protein at 7 mg/mL plus 300 nL reservoir: 100 mM bis-tris chloride buffer at pH 6.1, 23.6 (w/v) PEG 3350, 160 mM sodium thiocyanate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.95373 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 29, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.95373 Å / Relative weight: 1
ReflectionResolution: 1.59→45.9 Å / Num. obs: 139549 / % possible obs: 100 % / Redundancy: 13.5 % / CC1/2: 0.996 / Rmerge(I) obs: 0.183 / Rpim(I) all: 0.074 / Net I/σ(I): 8.2
Reflection shellResolution: 1.59→1.62 Å / Redundancy: 10.4 % / Rmerge(I) obs: 1.122 / Num. unique obs: 6791 / CC1/2: 0.665 / Rpim(I) all: 0.53 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6azn

6azn


Resolution: 1.59→45.9 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.962 / SU B: 1.413 / SU ML: 0.049 / Cross valid method: THROUGHOUT / ESU R: 0.071 / ESU R Free: 0.07 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.1742 6861 4.9 %RANDOM
Rwork0.15378 ---
obs0.15478 132605 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: 16.638 Å2
Baniso -1Baniso -2Baniso -3
1--0.36 Å2-0 Å20 Å2
2--0.62 Å2-0 Å2
3----0.25 Å2
Refinement stepCycle: 1 / Resolution: 1.59→45.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6967 0 104 888 7959
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0197513
X-RAY DIFFRACTIONr_bond_other_d0.0020.026968
X-RAY DIFFRACTIONr_angle_refined_deg1.7871.98310203
X-RAY DIFFRACTIONr_angle_other_deg1.069316192
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.095957
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.33523.667330
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.703151207
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.4881562
X-RAY DIFFRACTIONr_chiral_restr0.1140.21098
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0218432
X-RAY DIFFRACTIONr_gen_planes_other0.0020.021483
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_it1.3341.4833768
X-RAY DIFFRACTIONr_mcbond_other1.3311.4833767
X-RAY DIFFRACTIONr_mcangle_it1.9082.2224745
X-RAY DIFFRACTIONr_mcangle_other1.9082.2224746
X-RAY DIFFRACTIONr_scbond_it2.3531.7363745
X-RAY DIFFRACTIONr_scbond_other2.3521.7363745
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other3.5342.5165459
X-RAY DIFFRACTIONr_long_range_B_refined4.5529.56532857
X-RAY DIFFRACTIONr_long_range_B_other4.36628.95731810
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A149940.07
12B149940.07
21A154700.06
22C154700.06
31A150060.07
32D150060.07
41B149380.06
42C149380.06
51B151500.05
52D151500.05
61C148640.07
62D148640.07
LS refinement shellResolution: 1.59→1.631 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.252 501 -
Rwork0.237 9691 -
obs--99.99 %

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