2j91

X-ray diffraction
1.8Å resolution

Crystal structure of Human Adenylosuccinate Lyase in complex with AMP

Released:
Source organism: Homo sapiens
Entry authors: Stenmark P, Moche M, Arrowsmith C, Berglund H, Busam R, Collins R, Edwards A, Ericsson UB, Flodin S, Flores A, Graslund S, Hammarstrom M, Hallberg BM, Holmberg Schiavone L, Hogbom M, Johansson I, Karlberg T, Kosinska U, Kotenyova T, Magnusdottir A, Nilsson ME, Nilsson-Ehle P, Nyman T, Ogg D, Persson C, Sagemark J, Sundstrom M, Uppenberg J, Uppsten M, Thorsell AG, van Den Berg S, Wallden K, Weigelt J, Nordlund P

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

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: 503 amino acids
Theoretical weight: 57.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30566 (Residues: 1-481; Coverage: 99%)
Gene names: ADSL, AMPS
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P212121
Unit cell:
a: 85.37Å b: 104.342Å c: 213.396Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.157 0.199
Expression system: Escherichia coli BL21(DE3)