Structure analysis

Crystal structure of [NiFe] hydrogenase maturation protein, HypD from Thermococcus kodakaraensis

X-ray diffraction
2.07Å resolution
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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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
Accessible surface area: 15600 Å2
Buried surface area: 350 Å2
Dissociation area: 200 Å2
Dissociation energy (ΔGdiss): 10 kcal/mol
Dissociation entropy (TΔSdiss): 2 kcal/mol
Interface energy (ΔGint): -13 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B
Length: 372 amino acids
Theoretical weight: 41.96 KDa
Source organism: Thermococcus kodakarensis KOD1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5JII1 (Residues: 1-372; Coverage: 100%)
Gene names: TK2000, Tk-hypD
Pfam: Hydrogenase formation hypA family
InterPro:
CATH:

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