1hlp

X-ray diffraction
3.2Å resolution

STRUCTURAL FEATURES STABILIZING HALOPHILIC MALATE DEHYDROGENASE FROM AN ARCHAEBACTERIUM

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 32.71 KDa
Source organism: Haloarcula marismortui
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07841 (Residues: 2-304; Coverage: 100%)
Gene names: mdh, rrnAC2706
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 114.6Å b: 130.6Å c: 123.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.28
Expression system: Escherichia coli