Sodium in PDB 2bhc: Na Substituted E. Coli Aminopeptidase P

All present enzymatic activity of Na Substituted E. Coli Aminopeptidase P:
3.4.11.9;

The structure of Na Substituted E. Coli Aminopeptidase P, PDB code: 2bhc was solved by S.C.Graham, C.S.Bond, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.19 / 2.40
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	138.783, 138.783, 231.012, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 20.2

The structure of Na Substituted E. Coli Aminopeptidase P also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Sodium atom in the Na Substituted E. Coli Aminopeptidase P (pdb code 2bhc). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Na Substituted E. Coli Aminopeptidase P, PDB code: 2bhc:

Sodium binding site 1 out of 1 in the Na Substituted E. Coli Aminopeptidase P


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Na Substituted E. Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1441 b:43.8 occ:1.00 OE2 A:GLU406 2.3 50.9 1.0 NE2 A:HIS354 2.5 45.7 1.0 OD2 A:ASP271 2.5 51.2 1.0 OE2 A:GLU383 2.6 61.1 1.0 O A:HOH2030 2.6 51.6 1.0 O A:HOH2137 2.7 41.9 1.0 CD A:GLU406 3.2 48.0 1.0 CD A:GLU383 3.2 54.3 1.0 OE1 A:GLU383 3.3 61.4 1.0 CG A:ASP271 3.3 47.1 1.0 OE1 A:GLU406 3.4 50.7 1.0 CD2 A:HIS354 3.4 45.3 1.0 OD1 A:ASP271 3.5 52.6 1.0 CE1 A:HIS354 3.5 44.9 1.0 OG1 A:THR381 4.0 46.9 1.0 CG2 A:THR381 4.1 46.0 1.0 CB A:THR381 4.3 46.3 1.0 CG A:GLU383 4.6 52.1 1.0 ND1 A:HIS354 4.6 44.6 1.0 CG A:HIS354 4.6 44.4 1.0 CG A:GLU406 4.6 46.5 1.0 CB A:ASP271 4.7 46.3 1.0 NE2 A:HIS361 4.7 56.9 1.0 CD2 A:HIS361 5.0 54.9 1.0

S.C.Graham, C.S.Bond, H.C.Freeman, J.M.Guss. Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, A Metalloprotease with A Dinuclear Metal Center. Biochemistry V. 44 13820 2005.
ISSN: ISSN 0006-2960
PubMed: 16229471
DOI: 10.1021/BI0512849