› 4qlg

X-ray diffraction
1.5Å resolution

Crystal structure of I14V DHFR mutant complexed with folate and NADP+

Released:
DOI: 10.2210/pdb4qlg/pdb
PDB entry 4qlg coloured by chain, front view.
PDB entry 4qlg coloured by chain, side view.
PDB entry 4qlg coloured by chain, top view.
Source organism: Escherichia coli str. K-12 substr. MC4100
Primary publication:
Free energy simulations of active-site mutants of dihydrofolate reductase.
Doron D, Stojković V, Gakhar L, Vardi-Kilshtain A, Kohen A, Major DT
J Phys Chem B 119 906-16 (2015)
PMID: 25382260

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 18.01 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
Expression system: Escherichia coli
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments

2 bound ligands:
Ligand FOL 2 x FOL
Ligand NAP 2 x NAP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 35.077Å b: 60.253Å c: 74.179Å
α: 90° β: 95.97° γ: 90°
R-values:
R R work R free
0.176 0.174 0.227
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Engineered control of enzyme structural dynamics and function.
Boehr et al. (2018)
5 other articles

1 mention without citation

The role of the Met20 loop in the hydride transfer in Escherichia coli dihydrofolate reductase.
Mhashal et al. (2017)