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- PDB-1vhu: Crystal structure of a putative phosphoesterase -

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Basic information

Entry
Database: PDB / ID: 1vhu
TitleCrystal structure of a putative phosphoesterase
ComponentsHypothetical protein AF1521
KeywordsStructural genomics / unknown function
Function / homology
Function and homology information


peptidyl-glutamate ADP-deribosylation / ADP-ribosylglutamate hydrolase activity / Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds
Similarity search - Function
Leucine Aminopeptidase, subunit E, domain 1 / Leucine Aminopeptidase, subunit E; domain 1 / Macro domain / Appr-1"-p processing enzyme / Macro domain / Macro domain profile. / Macro domain-like / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ADP-ribose glycohydrolase AF_1521
Similarity search - Component
Biological speciesArchaeoglobus fulgidus (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Se-Met SAD phasing / Resolution: 1.34 Å
AuthorsStructural GenomiX
CitationJournal: Proteins / Year: 2005
Title: Structural analysis of a set of proteins resulting from a bacterial genomics project
Authors: Badger, J. / Sauder, J.M. / Adams, J.M. / Antonysamy, S. / Bain, K. / Bergseid, M.G. / Buchanan, S.G. / Buchanan, M.D. / Batiyenko, Y. / Christopher, J.A. / Emtage, S. / Eroshkina, A. / ...Authors: Badger, J. / Sauder, J.M. / Adams, J.M. / Antonysamy, S. / Bain, K. / Bergseid, M.G. / Buchanan, S.G. / Buchanan, M.D. / Batiyenko, Y. / Christopher, J.A. / Emtage, S. / Eroshkina, A. / Feil, I. / Furlong, E.B. / Gajiwala, K.S. / Gao, X. / He, D. / Hendle, J. / Huber, A. / Hoda, K. / Kearins, P. / Kissinger, C. / Laubert, B. / Lewis, H.A. / Lin, J. / Loomis, K. / Lorimer, D. / Louie, G. / Maletic, M. / Marsh, C.D. / Miller, I. / Molinari, J. / Muller-Dieckmann, H.J. / Newman, J.M. / Noland, B.W. / Pagarigan, B. / Park, F. / Peat, T.S. / Post, K.W. / Radojicic, S. / Ramos, A. / Romero, R. / Rutter, M.E. / Sanderson, W.E. / Schwinn, K.D. / Tresser, J. / Winhoven, J. / Wright, T.A. / Wu, L. / Xu, J. / Harris, T.J.
History
DepositionDec 1, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 30, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 4, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.4Dec 27, 2023Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Hypothetical protein AF1521
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,7212
Polymers23,5261
Non-polymers1951
Water5,008278
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)54.570, 60.966, 52.746
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11A-446-

HOH

21A-485-

HOH

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Components

#1: Protein Hypothetical protein AF1521


Mass: 23526.139 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Archaeoglobus fulgidus (archaea) / Gene: AF1521 / Production host: Escherichia coli (E. coli) / References: UniProt: O28751
#2: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 278 / 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: 1.86 Å3/Da / Density % sol: 34.04 %
Crystal grow
*PLUS
pH: 7.5 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetailsChemical formula
110 mMHEPES1droppH7.5
2150 mM1dropNaCl
310 mMmethionine1drop
410 %glycerol1drop
55 mMdithiothreitol1drop
610 mg/mlprotein1drop

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 32-ID / Wavelength: 0.9794 Å
DetectorType: MARRESEARCH / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9794 Å / Relative weight: 1
ReflectionResolution: 1.34→24.9 Å / Num. all: 38929 / Num. obs: 38929 / % possible obs: 97.9 % / Redundancy: 6.5 % / Rmerge(I) obs: 0.064 / Net I/σ(I): 13
Reflection shellResolution: 1.34→1.42 Å / Redundancy: 5 % / Rmerge(I) obs: 0.495 / Mean I/σ(I) obs: 3.2 / % possible all: 90.2
Reflection shell
*PLUS
% possible obs: 90.2 %

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
SCALAdata scaling
TRUNCATEdata reduction
REFMAC4refinement
CCP4(SCALAdata scaling
TRUNCATEdata scaling
RefinementMethod to determine structure: Se-Met SAD phasing / Resolution: 1.34→24.9 Å / σ(F): 0
RfactorNum. reflection
Rfree0.18 1951
Rwork0.151 -
obs-38929
Solvent computationSolvent model: Babinet bulk solvent correction / Bsol: 218.064 Å2 / ksol: 0.75 e/Å3
Displacement parametersBiso mean: 15.299 Å2
Baniso -1Baniso -2Baniso -3
1--0.111 Å20 Å20 Å2
2---0.241 Å20 Å2
3---0.352 Å2
Refine Biso Class: all / Treatment: anisotropic
Refinement stepCycle: LAST / Resolution: 1.34→24.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1488 0 12 278 1778
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONp_bond_d0.015
X-RAY DIFFRACTIONp_angle_d1.529
X-RAY DIFFRACTIONp_planar_tor5.74
X-RAY DIFFRACTIONp_chiral_restr0.111
X-RAY DIFFRACTIONp_plane_restr0.008
X-RAY DIFFRACTIONp_mcbond_it1.718
X-RAY DIFFRACTIONp_mcangle_it2.581
X-RAY DIFFRACTIONp_scbond_it3.494
X-RAY DIFFRACTIONp_scangle_it5.45
Software
*PLUS
Version: 4 / Classification: refinement
Refinement
*PLUS
Rfactor Rfree: 0.18
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONp_angle_d
X-RAY DIFFRACTIONp_angle_deg1.5

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