› 4q3m

X-ray diffraction
2.55Å resolution

Crystal structure of MGS-M4, an aldo-keto reductase enzyme from a Medee basin deep-sea metagenome library

Released:
DOI: 10.2210/pdb4q3m/pdb
Model geometry
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PDB entry 4q3m coloured by chain, front view.
PDB entry 4q3m coloured by chain, side view.
PDB entry 4q3m coloured by chain, top view.
Source organism: unidentified
Primary publication:
Pressure adaptation is linked to thermal adaptation in salt-saturated marine habitats.
Alcaide M, Stogios PJ, Lafraya Á, Tchigvintsev A, Flick R, Bargiela R, Chernikova TN, Reva ON, Hai T, Leggewie CC, Katzke N, La Cono V, Matesanz R, Jebbar M, Jaeger KE, Yakimov MM, Yakunin AF, Golyshin PN, Golyshina OV, Savchenko A, Ferrer M
Environ Microbiol 17 332-45 (2015)
PMID: 25330254

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101009 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADP-dependent oxidoreductase domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 274 amino acids
Theoretical weight: 31.83 KDa
Source organism: unidentified
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0B5KNF6 (Residues: 1-274; Coverage: 100%)
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

2 bound ligands:
Ligand SO4 6 x SO4
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P64
Unit cell:
a: 172.469Å b: 172.469Å c: 113.055Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.207 0.266
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Living at the Extremes: Extremophiles and the Limits of Life in a Planetary Context.
Merino et al. (2019)
3 more

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