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Crystal structure of a putative Aspartate Aminotransferase from Leishmania major Friedlin

X-ray diffraction
1.85Å resolution
PDB entry 4h51 coloured by chain, front view.
PDB entry 4h51 coloured by chain, side view.
PDB entry 4h51 coloured by chain, top view.
Source organism: Leishmania major strain Friedlin
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Aminotransferase class I/classII large domain-containing protein
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Multimeric state: homo dimer
Accessible surface area: 28057.94 Å2
Buried surface area: 7808.95 Å2
Dissociation area: 3,678.34 Å2
Dissociation energy (ΔGdiss): 37.7 kcal/mol
Dissociation entropy (TΔSdiss): 14.85 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-175522
Homo dimeric assembly 1 of PDB entry 4h51 coloured by chemically distinct molecules, front view.
Homo dimeric assembly 1 of PDB entry 4h51 coloured by chemically distinct molecules, side view.
Homo dimeric assembly 1 of PDB entry 4h51 coloured by chemically distinct molecules, top view.
    Assembly 1
Confidence : 98%
No. subunits : 2
Symmetry : C2
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3DComplex & QSbio predictionx
No. subunits : 2
Symmetry : C2
Evidence : Interface geometry is similar to that of 1bqa_1 (37% id)

Macromolecules

Aminotransferase class I/classII large domain-containing protein
Chains: A, B
Length: 420 amino acids
Theoretical weight: 47.3 KDa
Source organism: Leishmania major strain Friedlin
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4FX34 (Residues: 1-412; Coverage: 100%)
Gene names: LMJF_35_0820, asat
Pfam: Aminotransferase class I and II
InterPro:
CATH:
Aminotransferase class I/classII domain-containing protein in PDB entry 4h51, assembly 1, front view.
Aminotransferase class I/classII domain-containing protein in PDB entry 4h51, assembly 1, side view.
Aminotransferase class I/classII domain-containing protein in PDB entry 4h51, assembly 1, top view.
PDBe-KB: UniProt Coverage View: Q4FX34  
142050100150200250300350400
 
100200300400
UniProt
Q4FX34
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation
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