[English] 日本語
Yorodumi
- PDB-5scs: Crystal Structure of Dihydrofolate Reductase from Mycobacterium t... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5scs
TitleCrystal Structure of Dihydrofolate Reductase from Mycobacterium tuberculosis bound to NADP and SDDC Inhibitor SDDC-781
ComponentsDihydrofolate reductase
KeywordsOXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / Mycobacterium tuberculosis / DHFR / NADP / Folate / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID
Function / homology
Function and homology information


NADP+ binding / dihydrofolate metabolic process / dihydrofolate reductase / dihydrofolate reductase activity / folic acid metabolic process / tetrahydrofolate biosynthetic process / one-carbon metabolic process / NADP binding / cytosol
Similarity search - Function
Dihydrofolate reductase / Dihydrofolate reductase conserved site / Dihydrofolate reductase (DHFR) domain signature. / Dihydrofolate reductase (DHFR) domain profile. / Dihydrofolate reductase domain / Dihydrofolate reductase / Dihydrofolate reductase-like domain superfamily
Similarity search - Domain/homology
Chem-GYI / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Dihydrofolate reductase
Similarity search - Component
Biological speciesMycobacterium tuberculosis H37Rv (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.55 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)HHSN272201700059C United States
CitationJournal: to be published
Title: Crystal Structure of Dihydrofolate Reductase from Mycobacterium tuberculosis bound to NADP and SDDC Inhibitor SDDC-781
Authors: Mayclin, S.J. / Fairman, J.W. / Dranow, D.M. / Conrady, D.G. / Fox III, D. / Lukacs, C.M. / Lorimer, D.D. / Horanyi, P.S. / Edwards, T.E. / Abendroth, J.
History
DepositionDec 20, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 9, 2022Provider: repository / Type: Initial release
Revision 1.1Mar 2, 2022Group: Other / Structure summary
Category: pdbx_SG_project / pdbx_database_status / struct_keywords
Item: _pdbx_database_status.SG_entry / _struct_keywords.text
Revision 1.2May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Dihydrofolate reductase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,0413
Polymers19,8321
Non-polymers1,2092
Water3,207178
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)30.140, 66.000, 78.010
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Detailsbiological unit is a monomer, the same as asu

-
Components

#1: Protein Dihydrofolate reductase


Mass: 19832.365 Da / Num. of mol.: 1 / Fragment: MtDHFR
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis H37Rv (bacteria)
Strain: ATCC 25618 / H37Rv / Gene: folA, dfrA, Rv2763c, MTV002.28c / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P9WNX1, dihydrofolate reductase
#2: Chemical ChemComp-NAP / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE


Mass: 743.405 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H28N7O17P3
#3: Chemical ChemComp-GYI / 3-(2-{3-[(2,4-diamino-6-ethylpyrimidin-5-yl)oxy]propoxy}phenyl)-N-(propane-2-sulfonyl)propanamide


Mass: 465.566 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H31N5O5S / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 178 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 1.96 Å3/Da / Density % sol: 37.12 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop
Details: MCSG1 D4: 20% PEG3350, 200mM Sodium Thiocyanate pH6.9

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: FR-E+ Superbright / Wavelength: 1.5418 Å
DetectorType: Saturn 944+ / Detector: CCD / Date: Oct 12, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.55→50 Å / Num. obs: 22688 / % possible obs: 97.2 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 21.571 Å2 / Rmerge F obs: 0.999 / Rmerge(I) obs: 0.058 / Rrim(I) all: 0.06 / Net I/σ(I): 26.66 / Num. measured all: 318414
Reflection shell
Resolution (Å)Highest resolution (Å)Rmerge F obsRmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsRrim(I) all% possible all
1.55-1.590.8870.3883.818459171215670.42791.5
1.59-1.630.9480.3525.5714463160615150.37194.3
1.63-1.680.960.336.1716194165315670.34794.8
1.68-1.730.9730.2747.4716137154615310.28899
1.73-1.790.9830.2289.1316311152114620.23996.1
1.79-1.850.990.19110.5316635146114570.19999.7
1.85-1.920.990.14317.6615427140813860.1598.4
1.92-20.9950.14117.5815065140012550.14789.6
2-2.090.9970.10221.0817113130513050.106100
2.09-2.190.9980.09123.4517029127312700.09499.8
2.19-2.310.9930.09832.8713206119911560.10396.4
2.31-2.450.9990.07832.8217978112810960.0897.2
2.45-2.620.9990.05942.3419241108510840.06199.9
2.62-2.830.9990.05745.5819067101010090.05899.9
2.83-3.10.9990.04852.45192719379370.05100
3.1-3.4710.04564.53210958478470.046100
3.47-40.9990.04972.44184187617590.0599.7
4-4.910.03578.11168916596530.03699.1
4.9-6.9310.04173.64132745165160.042100
6.930.9980.03973.4771403173160.0499.7

-
Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
PHENIXdev_2219refinement
PDB_EXTRACT3.11data extraction
PHENIXmodel building
Cootmodel building
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.55→39.005 Å / Occupancy max: 1 / Occupancy min: 0.76 / SU ML: 0.16 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.24 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2453 1938 8.54 %
Rwork0.2077 20748 -
obs0.211 22686 97.18 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 75.78 Å2 / Biso mean: 19.2378 Å2 / Biso min: 5.69 Å2
Refinement stepCycle: LAST / Resolution: 1.55→39.005 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1289 0 80 178 1547
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0061407
X-RAY DIFFRACTIONf_angle_d1.0681925
X-RAY DIFFRACTIONf_chiral_restr0.054201
X-RAY DIFFRACTIONf_plane_restr0.005241
X-RAY DIFFRACTIONf_dihedral_angle_d18.997788
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.55-1.58870.22561280.21051380150892
1.5887-1.63170.24071340.19321385151994
1.6317-1.67970.27151260.19821441156795
1.6797-1.73390.24151370.21474161199
1.7339-1.79590.24981360.20221443157996
1.7959-1.86780.28211400.22711503164399
1.8678-1.95280.31461350.2991447158297
1.9528-2.05580.2981340.251419155394
2.0558-2.18460.2441420.208215081650100
2.1846-2.35320.39051380.32041471160996
2.3532-2.590.27261420.202615131655100
2.59-2.96460.23371450.196215421687100
2.9646-3.73470.20581460.17115701716100
3.7347-39.01730.16811550.151316521807100
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.8779-0.351-0.45542.03770.5880.30890.0020.0989-0.1304-0.0639-0.1992-0.06640.1557-0.12360.18930.10450.03620.02180.1239-0.01180.0976-10.0363-11.84676.3133
21.0474-0.3228-0.96660.7295-0.06541.20130.0163-0.01950.16220.2185-0.1375-0.2635-0.32070.5146-0.11980.074-0.0167-0.02610.27240.0320.1544-4.3795-1.60118.409
35.8037-2.01910.2284.4249-0.03052.64750.0475-0.16090.25570.1607-0.0516-0.2701-0.27120.3166-0.01930.1136-0.03670.00310.15010.02680.0517-3.26322.6955.8719
48.0644-2.52020.26146.023-0.31784.0414-0.01120.0920.430.08390.0348-0.044-0.54710.1229-0.03440.1612-0.00440.01720.14520.0180.0766-8.91317.4131-0.8563
51.23161.1155-0.96983.1708-0.6981.2197-0.01310.17990.0107-0.12160.08150.09420.0105-0.0399-0.06580.09670.033-0.01120.12090.00690.0806-13.7723-3.73152.6224
63.17761.16652.45833.03112.64296.81540.0722-0.0873-0.04980.39150.01380.02570.18420.0232-0.12510.0887-0.0171-0.0180.0749-0.00280.0643-10.2609-10.668115.7476
73.345-0.86532.05150.8638-0.48943.4148-0.1234-0.26180.33680.3398-0.0267-0.0373-0.3429-0.25110.10620.2240.02510.02030.2013-0.04290.126-14.71443.386926.4738
81.29781.64140.29544.16291.2892.00290.0641-0.3164-0.12960.2686-0.02270.39610.1099-0.23170.03740.0925-0.05660.00450.16390.03160.1315-17.5403-12.233616.6709
92.69771.13961.06071.67950.2310.62910.13610.0154-0.13710.183-0.0242-0.13130.2060.2828-0.04550.1245-0.0087-0.02270.13630.00980.1033-5.466-11.369723.5556
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid -6 through 9 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 10 through 35 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 36 through 60 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 61 through 76 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 77 through 106 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 107 through 115 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 116 through 125 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 126 through 139 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 140 through 159 )A0

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more