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- PDB-3o1c: High resolution crystal structure of histidine triad nucleotide-b... -

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Basic information

Entry
Database: PDB / ID: 3o1c
TitleHigh resolution crystal structure of histidine triad nucleotide-binding protein 1 (Hint1) C38A mutant from rabbit complexed with Adenosine
ComponentsHistidine triad nucleotide-binding protein 1
KeywordsHYDROLASE / HINT PROTEIN / HIT PROTEIN / ADENOSINE 5'-MONOPHOSPHORAMIDASE
Function / homology
Function and homology information


purine ribonucleotide catabolic process / Hydrolases; Acting on phosphorus-nitrogen bonds / adenosine 5'-monophosphoramidase activity / deSUMOylase activity / protein desumoylation / intrinsic apoptotic signaling pathway by p53 class mediator / histone deacetylase complex / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / hydrolase activity / nucleotide binding ...purine ribonucleotide catabolic process / Hydrolases; Acting on phosphorus-nitrogen bonds / adenosine 5'-monophosphoramidase activity / deSUMOylase activity / protein desumoylation / intrinsic apoptotic signaling pathway by p53 class mediator / histone deacetylase complex / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / hydrolase activity / nucleotide binding / regulation of DNA-templated transcription / proteolysis / nucleus / cytoplasm
Similarity search - Function
Histidine triad (HIT) protein / HIT domain / Histidine triad, conserved site / HIT domain signature. / HIT domain profile. / HIT-like domain / HIT-like / HIT family, subunit A / HIT-like superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENOSINE / Adenosine 5'-monophosphoramidase HINT1
Similarity search - Component
Biological speciesOryctolagus cuniculus (rabbit)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.08 Å
AuthorsDolot, R.M. / Ozga, M. / Krakowiak, A.K. / Nawrot, B. / Stec, W.J.
CitationJournal: J.Biol.Chem. / Year: 2010
Title: Histidine Triad Nucleotide-binding Protein 1 (HINT-1) Phosphoramidase Transforms Nucleoside 5'-O-Phosphorothioates to Nucleoside 5'-O-Phosphates.
Authors: Ozga, M. / Dolot, R. / Janicka, M. / Kaczmarek, R. / Krakowiak, A.
History
DepositionJul 21, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 4, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3Sep 6, 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_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _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

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Assembly

Deposited unit
A: Histidine triad nucleotide-binding protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)13,9954
Polymers13,6821
Non-polymers3133
Water3,675204
1
A: Histidine triad nucleotide-binding protein 1
hetero molecules

A: Histidine triad nucleotide-binding protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9908
Polymers27,3642
Non-polymers6266
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_555y,x,-z1
Buried area5380 Å2
ΔGint-52 kcal/mol
Surface area9500 Å2
MethodPISA
Unit cell
Length a, b, c (Å)39.965, 39.965, 141.700
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein Histidine triad nucleotide-binding protein 1 / Adenosine 5'-monophosphoramidase / P13.7


Mass: 13681.770 Da / Num. of mol.: 1 / Mutation: C38A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Gene: HINT1, HINT / Plasmid: pSGA02 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P80912, Hydrolases
#2: Chemical ChemComp-ADN / ADENOSINE


Mass: 267.241 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H13N5O4
#3: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 204 / 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: 2.07 Å3/Da / Density % sol: 40.51 %
Crystal growTemperature: 281 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 20% PEG 8000, 0.1M sodium acetate, 0.1M sodium cacodylate pH 6.5, protein concentration 10 mg/ml, VAPOR DIFFUSION, HANGING DROP, temperature 281K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.91841 Å
DetectorType: RAYONIX MX-225 / Detector: CCD / Date: Sep 17, 2009 / Details: mirrors
RadiationMonochromator: Si-111 crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91841 Å / Relative weight: 1
ReflectionResolution: 1.08→28.26 Å / Num. obs: 48586 / % possible obs: 96.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 19.9 % / Biso Wilson estimate: 9.5 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 26.3
Reflection shellResolution: 1.08→1.14 Å / Redundancy: 14.3 % / Rmerge(I) obs: 0.556 / Mean I/σ(I) obs: 5 / Num. unique all: 95611 / % possible all: 94.2

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Processing

Software
NameVersionClassification
MAR345data collection
MOLREP10.2.31phasing
REFMAC5.5.0109refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3LLJ

3llj
PDB Unreleased entry


Resolution: 1.08→28.26 Å / Cor.coef. Fo:Fc: 0.979 / Cor.coef. Fo:Fc free: 0.969 / SU B: 0.799 / SU ML: 0.018 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.03 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.16285 2481 5.1 %RANDOM
Rwork0.13182 ---
all0.13335 50494 --
obs0.13335 46067 96.15 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 20.525 Å2
Baniso -1Baniso -2Baniso -3
1-0.08 Å20 Å20 Å2
2--0.08 Å20 Å2
3----0.15 Å2
Refinement stepCycle: LAST / Resolution: 1.08→28.26 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms883 0 21 204 1108
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0280.0211111
X-RAY DIFFRACTIONr_angle_refined_deg2.3711.9811528
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.5415151
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.47724.66745
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.31615189
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.47154
X-RAY DIFFRACTIONr_chiral_restr0.1470.2161
X-RAY DIFFRACTIONr_gen_planes_refined0.0150.021885
X-RAY DIFFRACTIONr_mcbond_it3.3142695
X-RAY DIFFRACTIONr_mcangle_it4.87441140
X-RAY DIFFRACTIONr_scbond_it5.6214416
X-RAY DIFFRACTIONr_scangle_it7.3856388
X-RAY DIFFRACTIONr_rigid_bond_restr1.97211111
LS refinement shellResolution: 1.08→1.108 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.214 188 -
Rwork0.179 3183 -
obs-3183 92.15 %

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