› 3asv

X-ray diffraction
2.7Å resolution

The Closed form of serine dehydrogenase complexed with NADP+

Released:
DOI: 10.2210/pdb3asv/pdb
PDB 3asv coloured by chain and viewed from the front.
PDB 3asv coloured by chain and viewed from the side.
PDB 3asv coloured by chain and viewed from the top.
Source organism: Escherichia coli
Primary publication:
Crystal structure of serine dehydrogenase from Escherichia coli: important role of the C-terminal region for closed-complex formation.
Yamazawa R, Nakajima Y, Mushiake K, Yoshimoto T, Ito K
J. Biochem. 149 701-12 (2011)
PMID: 21349860

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Short-chain dehydrogenase/reductase SDR Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 248 amino acids
Theoretical weight: 27.28 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

2 bound ligands:
Ligand NAP 6 x NAP
Ligand PO4 6 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P64
Unit cell:
a: 113.859Å b: 113.859Å c: 197.54Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.192 0.273
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Biochemical studies and ligand-bound structures of biphenyl dehydrogenase from Pandoraea pnomenusa strain B-356 reveal a basis for broad specificity of the enzyme.
Dhindwal et al. (2011)
10 more

3 mentions without citation

Structure-based conversion of the coenzyme requirement of a short-chain dehydrogenase/reductase involved in bacterial alginate metabolism.
Takase et al. (2014)
2 more