› 2ano

X-ray diffraction
2.68Å resolution

Crystal structure of E.coli dihydrofolate reductase in complex with NADPH and the inhibitor MS-SH08-17

Released:
DOI: 10.2210/pdb2ano/pdb
PDB entry 2ano coloured by chain, front view.
PDB entry 2ano coloured by chain, side view.
PDB entry 2ano coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A 2.13 A structure of E. coli dihydrofolate reductase bound to a novel competitive inhibitor reveals a new binding surface involving the M20 loop region.
Summerfield RL, Daigle DM, Mayer S, Mallik D, Hughes DW, Jackson SG, Sulek M, Organ MG, Brown ED, Junop MS
J Med Chem 49 6977-86 (2006)
PMID: 17125251

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142189 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.02 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0ABQ4 (Residues: 1-159; Coverage: 100%)
Gene names: JW0047, b0048, folA, tmrA
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NDP 1 x NDP
2 bound ligands:
Ligand MN 1 x MN
Ligand 817 1 x 817
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 34.13Å b: 44.14Å c: 97.784Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.237 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Limitations and lessons in the use of X-ray structural information in drug design.
Davis et al. (2008)
24 other articles

2 mentions without citation

Protein rethreading: A novel approach to protein design.
Agah et al. (2016)
1 more