Structure analysis

ON THE ROLE OF LYSINE 166 IN THE MECHANISM OF MANDELATE RACEMASE FROM PSEUDOMONAS PUTIDA: MECHANISTIC AND CRYSTALLOGRAPHIC EVIDENCE FOR STEREOSPECIFIC ALKYLATION BY (R)-ALPHA-PHENYLGLYCIDATE

X-ray diffraction
2Å resolution
Source organism: Pseudomonas putida
Assembly composition:
homo octamer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo octamer
Accessible surface area: 83900 Å2
Buried surface area: 30500 Å2
Dissociation area: 7,200 Å2
Dissociation energy (ΔGdiss): 28 kcal/mol
Dissociation entropy (TΔSdiss): 47 kcal/mol
Interface energy (ΔGint): -215 kcal/mol
Symmetry number: 8

Macromolecules

Chain: A
Length: 357 amino acids
Theoretical weight: 38.38 KDa
Source organism: Pseudomonas putida
Expression system: Not provided
UniProt:
  • Best match: P11444 (Residues: 3-359)
Gene name: mdlA

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