Structure analysis

Crystal Structure Of Shikimate Kinase (aq_2177) From Aquifex Aeolicus vf5

X-ray diffraction
2.1Å resolution
Source organism: Aquifex aeolicus VF5
Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly
Assembly 3 (preferred)
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly
Assembly 4
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly
Assembly 5
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly
Assembly 6
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly
Assembly 7
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Multimeric state: monomeric
Accessible surface area: 8800 Å2
Buried surface area: 200 Å2
Dissociation area: 50 Å2
Dissociation energy (ΔGdiss): -2 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Interface energy (ΔGint): 2 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B, C, D
Length: 168 amino acids
Theoretical weight: 19.25 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O67925 (Residues: 1-168; Coverage: 100%)
Gene names: aq_2177, aroK
Pfam: Shikimate kinase
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases

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