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- PDB-1diu: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEX WITH BRODIMOPRIM-4,... -

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Basic information

Entry
Database: PDB / ID: 1diu
TitleDIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEX WITH BRODIMOPRIM-4,6-DICARBOXYLATE
ComponentsDIHYDROFOLATE REDUCTASE
KeywordsOXIDOREDUCTASE / INHIBITOR-ENZYME COMPLEX / OXIDO-REDUCTASE
Function / homology
Function and homology information


response to methotrexate / dihydrofolate metabolic process / dihydrofolate reductase / dihydrofolate reductase activity / folic acid metabolic process / tetrahydrofolate biosynthetic process / one-carbon metabolic process / NADP binding / response to antibiotic / cytosol
Similarity search - Function
Dihydrofolate reductase / Dihydrofolate Reductase, subunit A / Dihydrofolate Reductase, subunit A / Dihydrofolate reductase conserved site / Dihydrofolate reductase (DHFR) domain signature. / Dihydrofolate reductase (DHFR) domain profile. / Dihydrofolate reductase domain / Dihydrofolate reductase / Dihydrofolate reductase-like domain superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
BRODIMOPRIM-4,6-DICARBOXYLATE / Dihydrofolate reductase
Similarity search - Component
Biological speciesLactobacillus casei (bacteria)
MethodSOLUTION NMR
AuthorsMorgan, W.D. / Birdsall, B. / Polshakov, V.I. / Sali, D. / Kompis, I. / Feeney, J.
Citation
Journal: Biochemistry / Year: 1995
Title: Solution structure of a brodimoprim analogue in its complex with Lactobacillus casei dihydrofolate reductase.
Authors: Morgan, W.D. / Birdsall, B. / Polshakov, V.I. / Sali, D. / Kompis, I. / Feeney, J.
#1: Journal: Biochemistry / Year: 1994
Title: Solution Structure of Bound Trimethoprim in its Complex with Lactobacillus Casei Dihydrofolate Reductase
Authors: Martorell, G. / Gradwell, M.J. / Birdsall, B. / Bauer, C.J. / Frenkiel, T.A. / Cheung, H.T.A. / Polshakov, V.I. / Kuyper, L. / Feeney, J.
#2: Journal: J.Med.Chem. / Year: 1984
Title: A 1H NMR Study of the Interactions and Conformations of Rationally Designed Brodimoprim Analogues in Complexes with Lactobacillus Casei Dihydrofolate Reductase
Authors: Birdsall, B. / Feeney, J. / Pascual, C. / Roberts, G.C.K. / Kompis, I. / Then, R.L. / Mueller, K. / Kroehn, A.
#3: Journal: J.Biol.Chem. / Year: 1982
Title: Crystal Structures of Escherichia Coli and Lactobacillus Casei Dihydrofolate Reductase Refined at 1.7 Angstroms Resolution. I. General Features and Binding of Methotrexate
Authors: Bolin, J.T. / Filman, D.J. / Matthews, D.A. / Hamlin, R.C. / Kraut, J.
History
DepositionAug 1, 1995Processing site: BNL
Revision 1.0Nov 14, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Structure summary
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_keywords / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name / _struct_keywords.text / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: DIHYDROFOLATE REDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,8282
Polymers18,3321
Non-polymers4961
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: CIS PROLINE - PRO 53
2: GLY 98 - GLY 99 OMEGA = 2.29 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
3: THR 34 - VAL 35 MODEL 3 OMEGA = 143.95 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
4: THR 34 - VAL 35 MODEL 7 OMEGA = 137.21 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
5: THR 34 - VAL 35 MODEL 9 OMEGA = 135.63 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
6: THR 34 - VAL 35 MODEL 12 OMEGA = 143.15 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)18 / -
Representative

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Components

#1: Protein DIHYDROFOLATE REDUCTASE


Mass: 18331.594 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lactobacillus casei (bacteria) / Strain: METHOTREXATE-RESISTANT / Gene: POTENTIAL / Production host: Escherichia coli (E. coli) / References: UniProt: P00381, dihydrofolate reductase
#2: Chemical ChemComp-BDM / BRODIMOPRIM-4,6-DICARBOXYLATE


Mass: 496.332 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C20H24BrN4O6

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other

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Processing

NMR softwareName: Discover / Classification: refinement
NMR ensembleConformers submitted total number: 18

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