› › Structure analysis

Human JMJD5 in complex with MN and 5-((4-methoxybenzyl)amino)pyridine-2,4-dicarboxylic acid.

X-ray diffraction
1.62Å resolution
PDB entry 7dyt coloured by chain, front view.
PDB entry 7dyt coloured by chain, side view.
PDB entry 7dyt coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Bifunctional peptidase and arginyl-hydroxylase JMJD5
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Multimeric state: monomeric
Accessible surface area: 11256.43 Å2
Buried surface area: 124.44 Å2
Dissociation area: 62.22 Å2
Dissociation energy (ΔGdiss): 6.16 kcal/mol
Dissociation entropy (TΔSdiss): -0.13 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-185372

Macromolecules

Bifunctional peptidase and arginyl-hydroxylase JMJD5
Chain: A
Length: 235 amino acids
Theoretical weight: 27.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8N371 (Residues: 183-416; Coverage: 56%)
Gene names: JMJD5, KDM8
Pfam: Cupin-like domain
InterPro:
Bifunctional peptidase and arginyl-hydroxylase JMJD5 in PDB entry 7dyt, assembly 1, front view.
Bifunctional peptidase and arginyl-hydroxylase JMJD5 in PDB entry 7dyt, assembly 1, side view.
Bifunctional peptidase and arginyl-hydroxylase JMJD5 in PDB entry 7dyt, assembly 1, top view.
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