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- PDB-3bmn: Structure of Pteridine Reductase 1 (PTR1) from Trypanosoma brucei... -

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Basic information

Entry
Database: PDB / ID: 3bmn
TitleStructure of Pteridine Reductase 1 (PTR1) from Trypanosoma brucei in ternary complex with cofactor (NADP+) and inhibitor (Compound AX3)
Components(Pteridine reductase) x 2
KeywordsOXIDOREDUCTASE / pteridine reductase / ptr1 / trypanosoma brucei / short chain dehydrogenase / inhibitor
Function / homology
Function and homology information


pteridine reductase activity / nucleotide binding
Similarity search - Function
Pteridine reductase / Short-chain dehydrogenase/reductase, conserved site / Short-chain dehydrogenases/reductases family signature. / Enoyl-(Acyl carrier protein) reductase / Short-chain dehydrogenase/reductase SDR / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / N~2~-cyclopropyl-1,3,5-triazine-2,4,6-triamine / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Pteridine reductase
Similarity search - Component
Biological speciesTrypanosoma brucei brucei (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.98 Å
AuthorsMartini, V.P. / Iulek, J. / Tulloch, L.B. / Hunter, W.N.
CitationJournal: J.Med.Chem. / Year: 2010
Title: Structure-based design of pteridine reductase inhibitors targeting african sleeping sickness and the leishmaniases.
Authors: Tulloch, L.B. / Martini, V.P. / Iulek, J. / Huggan, J.K. / Lee, J.H. / Gibson, C.L. / Smith, T.K. / Suckling, C.J. / Hunter, W.N.
History
DepositionDec 13, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 16, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.2Mar 26, 2025Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_conn / struct_ncs_dom_lim / 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_conn.pdbx_leaving_atom_flag / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _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

Downloads & links

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Assembly

Deposited unit
A: Pteridine reductase
B: Pteridine reductase
C: Pteridine reductase
D: Pteridine reductase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)127,13122
Polymers122,6954
Non-polymers4,43618
Water9,728540
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22620 Å2
MethodPISA
Unit cell
Length a, b, c (Å)73.840, 87.500, 84.230
Angle α, β, γ (deg.)90.000, 116.080, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51A
61B
71C
81D
91A
101B
111C
121D
131A
141B
151C
161D

NCS domain segments:

Ens-ID: 1 / Refine code: 3

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ALAALALEULEUAA3 - 10223 - 122
21ALAALALEULEUBB3 - 10223 - 122
31ALAALALEULEUCC3 - 10223 - 122
41ALAALALEULEUDD3 - 10223 - 122
52LYSLYSARGARGAA114 - 141134 - 161
62LYSLYSARGARGBB114 - 141134 - 161
72LYSLYSARGARGCC114 - 141134 - 161
82LYSLYSARGARGDD114 - 141134 - 161
93ASNASNLEULEUAA153 - 208173 - 228
103ASNASNLEULEUBB153 - 208173 - 228
113ASNASNLEULEUCC153 - 208173 - 228
123ASNASNLEULEUDD153 - 208173 - 228
134TRPTRPALAALAAA221 - 268241 - 288
144TRPTRPALAALABB221 - 268241 - 288
154TRPTRPALAALACC221 - 268241 - 288
164TRPTRPALAALADD221 - 268241 - 288

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein Pteridine reductase


Mass: 30685.787 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Gene: PTR1 / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O76290
#2: Protein Pteridine reductase


Mass: 30669.791 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Gene: PTR1 / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O76290

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Non-polymers , 6 types, 558 molecules

#3: Chemical
ChemComp-NAP / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE


Mass: 743.405 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C21H28N7O17P3
#4: Chemical
ChemComp-AX3 / N~2~-cyclopropyl-1,3,5-triazine-2,4,6-triamine


Mass: 166.184 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H10N6
#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#7: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H3O2
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 540 / 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: 1.99 Å3/Da / Density % sol: 38.25 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.5
Details: 2-3M sodium acetate, 10-100mM sodium citrate, pH 4.5, vapor diffusion, hanging drop, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 1.98→75.59 Å / Num. obs: 64386 / % possible obs: 95.8 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 26.881 Å2 / Rmerge(I) obs: 0.073 / Net I/σ(I): 14.12
Reflection shell
Resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obsDiffraction-ID% possible all
1.98-2.040.3434.1186625234191.5
2.04-2.10.295.2189194856195.2
2.1-2.180.2565.8220745653195.2
2.18-2.270.1897.6213015458195.6
2.27-2.370.1797.9201845167195.6
2.37-2.490.1479.2201025152195.7
2.49-2.650.12610.6215225517196.2
2.65-2.860.09613.3215925552196.7
2.86-3.140.06917.2203255250196.8
3.14-3.60.04822.5210205486196.9
3.6-4.530.03429.4206325466197.2

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACT3.004data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.98→75.59 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.904 / SU B: 6.938 / SU ML: 0.185 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.234 / ESU R Free: 0.203 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS All of the 17 related structures are expressed from the same DNA construct, which encodes CYS at positions 59 and 168. Crystals harvested ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS All of the 17 related structures are expressed from the same DNA construct, which encodes CYS at positions 59 and 168. Crystals harvested within a couple of days of formation contain CYS at positions 59 and 168. However these two residues appear quite reactive and over time become oxidised to CSX, as determined by the emergence in older crystals of electron density for the OD atom. Sometimes CYS168 reacts with DTT in the crystallisation buffer, covalently linking the two molecules by an S-S bond
RfactorNum. reflection% reflectionSelection details
Rfree0.267 3209 5 %RANDOM
Rwork0.206 ---
obs0.209 64384 96 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 24.048 Å2
Baniso -1Baniso -2Baniso -3
1--2.63 Å20 Å2-1.84 Å2
2--3.73 Å20 Å2
3----2.72 Å2
Refinement stepCycle: LAST / Resolution: 1.98→75.59 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7501 0 292 540 8333
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0228083
X-RAY DIFFRACTIONr_bond_other_d0.0010.027499
X-RAY DIFFRACTIONr_angle_refined_deg2.0282.00611035
X-RAY DIFFRACTIONr_angle_other_deg1.0433.00117389
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.19551051
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.6924.295312
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.078151305
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.8691551
X-RAY DIFFRACTIONr_chiral_restr0.1070.21309
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.028912
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021495
X-RAY DIFFRACTIONr_nbd_refined0.2250.22121
X-RAY DIFFRACTIONr_nbd_other0.1930.28556
X-RAY DIFFRACTIONr_nbtor_refined0.1880.23985
X-RAY DIFFRACTIONr_nbtor_other0.0920.25177
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2160.2587
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2220.223
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2160.290
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.250.29
X-RAY DIFFRACTIONr_mcbond_it1.5426545
X-RAY DIFFRACTIONr_mcbond_other0.23422079
X-RAY DIFFRACTIONr_mcangle_it1.91938182
X-RAY DIFFRACTIONr_scbond_it3.6614.53388
X-RAY DIFFRACTIONr_scangle_it4.78362813
Refine LS restraints NCS

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

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A1312TIGHT POSITIONAL0.050.05
2B1312TIGHT POSITIONAL0.060.05
3C1312TIGHT POSITIONAL0.060.05
4D1312TIGHT POSITIONAL0.050.05
1A1741LOOSE POSITIONAL0.75
2B1741LOOSE POSITIONAL0.765
3C1741LOOSE POSITIONAL0.775
4D1741LOOSE POSITIONAL0.75
1A1312TIGHT THERMAL0.070.25
2B1312TIGHT THERMAL0.070.25
3C1312TIGHT THERMAL0.060.25
4D1312TIGHT THERMAL0.070.25
1A1741LOOSE THERMAL1.575
2B1741LOOSE THERMAL1.745
3C1741LOOSE THERMAL1.555
4D1741LOOSE THERMAL1.575
LS refinement shellResolution: 1.98→2.031 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.36 212 -
Rwork0.313 4262 -
all-4474 -
obs--90.93 %

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