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- PDB-5ed6: crystal structure of human Hint1 H114A mutant complexing with ATP -

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Basic information

Entry
Database: PDB / ID: 5ed6
Titlecrystal structure of human Hint1 H114A mutant complexing with ATP
ComponentsHistidine triad nucleotide-binding protein 1
KeywordsHYDROLASE / nucleotide binding / regulation of transcription / signal transduction
Function / homology
Function and homology information


purine ribonucleotide catabolic process / Hydrolases; Acting on phosphorus-nitrogen bonds / adenosine 5'-monophosphoramidase activity / deSUMOylase activity / protein desumoylation / histone deacetylase complex / intrinsic apoptotic signaling pathway by p53 class mediator / positive regulation of calcium-mediated signaling / protein kinase C binding / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases ...purine ribonucleotide catabolic process / Hydrolases; Acting on phosphorus-nitrogen bonds / adenosine 5'-monophosphoramidase activity / deSUMOylase activity / protein desumoylation / histone deacetylase complex / intrinsic apoptotic signaling pathway by p53 class mediator / positive regulation of calcium-mediated signaling / protein kinase C binding / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / cytoskeleton / hydrolase activity / nucleotide binding / regulation of DNA-templated transcription / signal transduction / proteolysis / extracellular exosome / nucleoplasm / nucleus / plasma membrane / cytosol / 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 MONOPHOSPHATE / Adenosine 5'-monophosphoramidase HINT1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.52 Å
AuthorsWang, J. / Fang, P. / Guo, M.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM100136 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM106134 United States
CitationJournal: Nat Commun / Year: 2019
Title: Second messenger Ap4A polymerizes target protein HINT1 to transduce signals in Fc epsilon RI-activated mast cells.
Authors: Yu, J. / Liu, Z. / Liang, Y. / Luo, F. / Zhang, J. / Tian, C. / Motzik, A. / Zheng, M. / Kang, J. / Zhong, G. / Liu, C. / Fang, P. / Guo, M. / Razin, E. / Wang, J.
History
DepositionOct 20, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 25, 2017Provider: repository / Type: Initial release
Revision 1.1Apr 17, 2019Group: Author supporting evidence / Data collection / Derived calculations
Category: pdbx_audit_support / pdbx_struct_special_symmetry
Item: _pdbx_audit_support.funding_organization / _pdbx_audit_support.grant_number
Revision 1.2Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Apr 8, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.4Sep 27, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)28,5004
Polymers27,9142
Non-polymers5862
Water5,441302
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4670 Å2
ΔGint-20 kcal/mol
Surface area9540 Å2
MethodPISA
Unit cell
Length a, b, c (Å)78.356, 46.385, 64.077
Angle α, β, γ (deg.)90.000, 94.700, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11B-202-

EPE

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Components

#1: Protein Histidine triad nucleotide-binding protein 1 / Adenosine 5'-monophosphoramidase / Protein kinase C inhibitor 1 / Protein kinase C-interacting ...Adenosine 5'-monophosphoramidase / Protein kinase C inhibitor 1 / Protein kinase C-interacting protein 1 / PKCI-1


Mass: 13957.096 Da / Num. of mol.: 2 / Mutation: H114A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HINT1, HINT, PKCI1, PRKCNH1 / Production host: Escherichia coli (E. coli) / References: UniProt: P49773, Hydrolases
#2: Chemical ChemComp-AMP / ADENOSINE MONOPHOSPHATE / Adenosine monophosphate


Mass: 347.221 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H14N5O7P / Comment: AMP*YM
#3: Chemical ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES / HEPES


Mass: 238.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18N2O4S / Comment: pH buffer*YM
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 302 / 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: 2.08 Å3/Da / Density % sol: 40.83 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: PEG3350, HEPES

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97857 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jul 6, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97857 Å / Relative weight: 1
ReflectionResolution: 1.52→32.161 Å / Num. obs: 35261 / % possible obs: 100 % / Redundancy: 6.4 % / Biso Wilson estimate: 13.25 Å2 / Rmerge(I) obs: 0.051 / Χ2: 1 / Net I/av σ(I): 30.071 / Net I/σ(I): 13.8 / Num. measured all: 224835
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2% possible all
1.52-1.575.60.19535120.909100
1.57-1.646.40.16534840.951100
1.64-1.716.40.13434960.933100
1.71-1.86.40.10735230.937100
1.8-1.926.50.08635020.999100
1.92-2.066.50.0835421.32100
2.06-2.276.50.06335051.192100
2.27-2.66.50.05135301.029100
2.6-3.276.50.04835561.17100
3.27-506.40.02836110.54599.7

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Processing

Software
NameVersionClassification
HKL-2000data scaling
PHENIX1.9_1692refinement
PDB_EXTRACT3.15data extraction
HKL-2000data reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4EQE

4eqe


Resolution: 1.52→32.161 Å / SU ML: 0.11 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 16.08 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1639 1747 5.01 %
Rwork0.143 33114 -
obs0.1441 34861 98.4 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 56.54 Å2 / Biso mean: 17.2514 Å2 / Biso min: 7.33 Å2
Refinement stepCycle: final / Resolution: 1.52→32.161 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1744 0 31 302 2077
Biso mean--18.81 30.23 -
Num. residues----228
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0061837
X-RAY DIFFRACTIONf_angle_d1.1922490
X-RAY DIFFRACTIONf_chiral_restr0.049269
X-RAY DIFFRACTIONf_plane_restr0.006323
X-RAY DIFFRACTIONf_dihedral_angle_d14.525679
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.5203-1.57460.20481290.16042849297885
1.5746-1.63760.17751750.14353304347999
1.6376-1.71220.17071650.143733503515100
1.7122-1.80240.17211710.146533583529100
1.8024-1.91530.16271750.143633573532100
1.9153-2.06320.15641750.143533693544100
2.0632-2.27080.17331760.145533573533100
2.2708-2.59920.17911840.151733583542100
2.5992-3.27430.15821940.149633923586100
3.2743-32.16790.15192030.130434203623100
Refinement TLS params.Method: refined / Origin x: 13.1859 Å / Origin y: 1.0106 Å / Origin z: 16.3277 Å
111213212223313233
T0.0737 Å20.0017 Å2-0.0016 Å2-0.0853 Å2-0.0021 Å2--0.1039 Å2
L0.2096 °20.0401 °2-0.0625 °2-0.559 °2-0.0223 °2--1.4217 °2
S-0.0005 Å °0.0185 Å °-0.0019 Å °0.006 Å °-0.0067 Å °0.0211 Å °0.041 Å °-0.0318 Å °0.0087 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1allA14 - 126
2X-RAY DIFFRACTION1allB12 - 126
3X-RAY DIFFRACTION1allC1
4X-RAY DIFFRACTION1allE1 - 405
5X-RAY DIFFRACTION1allD1

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