› 4ffx

X-ray diffraction
2.7Å resolution

Structural and Biochemical Characterization of Human Adenylosuccinate Lyase (ADSL) and the R303C ADSL Deficiency Associated Mutation

Released:
DOI: 10.2210/pdb4ffx/pdb
PDB entry 4ffx coloured by chain, front view.
PDB entry 4ffx coloured by chain, side view.
PDB entry 4ffx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation.
Ray SP, Deaton MK, Capodagli GC, Calkins LA, Sawle L, Ghosh K, Patterson D, Pegan SD
Biochemistry 51 6701-13 (2012)
PMID: 22812634

Function and Biology Details

Reaction catalysed: 
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylosuccinate lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 487 amino acids
Theoretical weight: 55.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30566 (Residues: 1-484; Coverage: 100%)
Gene names: ADSL, AMPS
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 85.919Å b: 105.153Å c: 214.928Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.243 0.292
Expression system: Escherichia coli

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Citations

1 review citation

Human de novo purine biosynthesis.
Pareek et al. (2021)
9 other articles

2 mentions without citation

Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation.
Ray et al. (2012)
1 more