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- PDB-2e2k: Helicobacter pylori formamidase AmiF contains a fine-tuned cystei... -

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Basic information

Entry
Database: PDB / ID: 2e2k
TitleHelicobacter pylori formamidase AmiF contains a fine-tuned cysteine-glutamate-lysine catalytic triad
ComponentsFormamidase
KeywordsHYDROLASE / Formamidase / AmiF / CEK / catalytic triad / Helicobacter pylori / aliphatic amidase / C166S
Function / homology
Function and homology information


formamidase / formamidase activity / N-carbamoylputrescine amidase activity / putrescine biosynthetic process from arginine
Similarity search - Function
Formamidase / : / Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase / Carbon-nitrogen hydrolase / Carbon-nitrogen hydrolase domain profile. / Carbon-nitrogen hydrolase superfamily / Carbon-nitrogen hydrolase / Carbon-nitrogen hydrolase / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesHelicobacter pylori (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsWang, W.C. / Hung, C.L.
CitationJournal: J.Biol.Chem. / Year: 2007
Title: Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad
Authors: Hung, C.-L. / Liu, J.-H. / Chiu, W.-C. / Huang, S.-W. / Hwang, J.-K. / Wang, W.-C.
History
DepositionNov 14, 2006Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 13, 2007Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.3Nov 10, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Oct 25, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)223,8866
Polymers223,8866
Non-polymers00
Water15,313850
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area30740 Å2
ΔGint-164 kcal/mol
Surface area58150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)117.717, 130.527, 144.589
Angle α, β, γ (deg.)90.00, 99.44, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21A
12D
22A
13E
23A
14B
24B
15C
25B
16F
26B

NCS domain segments:

Component-ID: 1 / Beg auth comp-ID: GLY / Beg label comp-ID: GLY / End auth comp-ID: LYS / End label comp-ID: LYS / Refine code: 6 / Auth seq-ID: 13 - 334 / Label seq-ID: 13 - 334

Dom-IDEns-IDAuth asym-IDLabel asym-ID
11AA
21AA
12DD
22AA
13EE
23AA
14BB
24BB
15CC
25BB
16FF
26BB

NCS ensembles :
ID
1
2
3
4
5
6

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Components

#1: Protein
Formamidase / Formamide amidohydrolase / AmiF


Mass: 37314.332 Da / Num. of mol.: 6 / Mutation: C166S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Helicobacter pylori (bacteria) / Strain: 26695 / Gene: amiF / Plasmid: pQE30 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: O25836, formamidase
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 850 / Source method: isolated from a natural source / Formula: H2O

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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: 2.45 Å3/Da / Density % sol: 49.74 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5
Details: 0.2M lithium sulfate, 0.1M sodium acetate, 14% PEG 2000 MME, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 113 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL12B2 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: May 22, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 2.4→30 Å / Num. all: 84077 / Num. obs: 70795 / % possible obs: 99.84 % / Redundancy: 3.3 %
Reflection shellResolution: 2.4→2.49 Å / % possible all: 99.8

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2DYU

2dyu


Resolution: 2.5→30 Å / Cor.coef. Fo:Fc: 0.853 / Cor.coef. Fo:Fc free: 0.805 / SU B: 8.348 / SU ML: 0.198 / Cross valid method: THROUGHOUT / ESU R: 0.924 / ESU R Free: 0.352 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.29378 3788 5.1 %RANDOM
Rwork0.25564 ---
obs0.2576 70795 99.84 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 9.46 Å2
Baniso -1Baniso -2Baniso -3
1-0.03 Å20 Å2-0.1 Å2
2---0.58 Å20 Å2
3---0.52 Å2
Refinement stepCycle: LAST / Resolution: 2.5→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14894 0 0 850 15744
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.02215310
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg0.8821.94820783
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.38451856
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.14724.368712
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.852152454
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.2071564
X-RAY DIFFRACTIONr_chiral_restr0.0640.22171
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0211816
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2060.38623
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3210.510398
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2250.51709
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1590.340
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1730.58
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.2291.59529
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.414214966
X-RAY DIFFRACTIONr_scbond_it0.34636760
X-RAY DIFFRACTIONr_scangle_it0.5834.55817
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A2482loose positional08
2D2442loose positional0.548
3E2470loose positional0.548
4B2485loose positional08
5C2469loose positional0.448
6F2467loose positional0.418
1A2482loose thermal010
2D2442loose thermal1.0510
3E2470loose thermal1.110
4B2485loose thermal010
5C2469loose thermal0.9110
6F2467loose thermal1.2710
LS refinement shellResolution: 2.497→2.562 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.358 288 -
Rwork0.259 5105 -
obs--98.97 %

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