› 4pst

X-ray diffraction
1.05Å resolution

Multiconformer model for Escherichia coli dihydrofolate reductase at 277 K

Released:
DOI: 10.2210/pdb4pst/pdb
PDB entry 4pst coloured by chain, front view.
PDB entry 4pst coloured by chain, side view.
PDB entry 4pst coloured by chain, top view.
Source organism: Escherichia coli str. K-12 substr. MC4100
Primary publication:
Crystal cryocooling distorts conformational heterogeneity in a model Michaelis complex of DHFR.
Keedy DA, van den Bedem H, Sivak DA, Petsko GA, Ringe D, Wilson MA, Fraser JS
Structure 22 899-910 (2014)
PMID: 24882744

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-165054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.05 KDa
Source organism: Escherichia coli str. K-12 substr. MC4100
Expression system: Escherichia coli
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments

3 bound ligands:
Ligand FOL 1 x FOL
Ligand NAP 1 x NAP
Ligand MN 2 x MN
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 34.299Å b: 45.521Å c: 98.711Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.127 0.121 0.142
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Integrative, dynamic structural biology at atomic resolution--it's about time.
van den Bedem et al. (2015)
6 more

3 mentions without citation

Functional characterization of IS1999, an IS4 family element involved in mobilization and expression of beta-lactam resistance genes.
Aubert et al. (2006)
2 more