Structure analysis

Gly156Asp mutant of Human UroD, human uroporphyrinogen III decarboxylase

X-ray diffraction
2.2Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 26735.99 Å2
Buried surface area: 2420.22 Å2
Dissociation area: 1,210.11 Å2
Dissociation energy (ΔGdiss): 1.27 kcal/mol
Dissociation entropy (TΔSdiss): 13.9 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-138879
    Assembly 1
Confidence : 98%
No. subunits : 2
Symmetry : C2
3DComplex & QSbio predictionx
No. subunits : 2
Symmetry : C2

Macromolecules

Chain: A
Length: 388 amino acids
Theoretical weight: 43.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06132 (Residues: 1-367; Coverage: 100%)
Gene name: UROD
Pfam: Uroporphyrinogen decarboxylase (URO-D)
InterPro:
CATH: TIM Barrel
SCOP: Uroporphyrinogen decarboxylase, UROD
PDBe-KB: UniProt Coverage View: P06132  
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