2glj

X-ray diffraction
3.2Å resolution

crystal structure of aminopeptidase I from Clostridium acetobutylicum

Released:
Source organism: Clostridium acetobutylicum
Entry authors: Min T, Shapiro L, Burley SK, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable M18 family aminopeptidase 1 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 461 amino acids
Theoretical weight: 51.66 KDa
Source organism: Clostridium acetobutylicum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97K30 (Residues: 5-465; Coverage: 99%)
Gene names: CA_C1091, apeA
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P1
Unit cell:
a: 121.708Å b: 129.68Å c: 222.728Å
α: 89.88° β: 90° γ: 116.68°
R-values:
R R work R free
0.25 0.25 0.297
Expression system: Escherichia coli