› 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 4qlg coloured by chain and viewed from the front.
PDB 4qlg coloured by chain and viewed from the side.
PDB 4qlg coloured by chain and viewed from the top.
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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (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)