Manganese in PDB 1pdz: X-Ray Structure and Catalytic Mechanism of Lobster Enolase

All present enzymatic activity of X-Ray Structure and Catalytic Mechanism of Lobster Enolase:
4.2.1.11;

The structure of X-Ray Structure and Catalytic Mechanism of Lobster Enolase, PDB code: 1pdz was solved by J.Janin, S.Duquerroy, C.Camus, G.Le Bras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.20
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	110.800, 110.800, 73.400, 90.00, 90.00, 120.00
R / Rfree (%)	21.5 / n/a

The binding sites of Manganese atom in the X-Ray Structure and Catalytic Mechanism of Lobster Enolase (pdb code 1pdz). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the X-Ray Structure and Catalytic Mechanism of Lobster Enolase, PDB code: 1pdz:

Manganese binding site 1 out of 1 in the X-Ray Structure and Catalytic Mechanism of Lobster Enolase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of X-Ray Structure and Catalytic Mechanism of Lobster Enolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn440 b:42.2 occ:1.00 O A:HOH441 2.1 29.1 1.0 O A:HOH443 2.1 45.1 1.0 O A:HOH442 2.3 62.2 1.0 OD2 A:ASP319 2.3 44.8 1.0 OD2 A:ASP244 2.4 43.2 1.0 OE2 A:GLU294 2.4 27.6 1.0 OD1 A:ASP244 3.1 34.8 1.0 CG A:ASP244 3.1 37.5 1.0 CG A:ASP319 3.1 47.6 1.0 CD A:GLU294 3.4 32.4 1.0 CB A:ASP319 3.5 38.9 1.0 CG A:GLU294 4.1 31.4 1.0 OD2 A:ASP295 4.1 39.1 1.0 OD1 A:ASP319 4.2 54.0 1.0 NZ A:LYS395 4.2 19.0 1.0 OE1 A:GLU294 4.3 26.3 1.0 O A:HOH546 4.4 56.8 1.0 OE2 A:GLU166 4.4 29.9 1.0 CB A:ASP244 4.6 33.9 1.0 O2 A:PGA439 4.6 31.9 0.5 NZ A:LYS344 4.7 31.2 1.0 O A:HOH566 4.8 34.6 1.0 CD2 A:LEU342 4.8 24.5 1.0 CG A:ASP295 4.9 35.2 1.0 CA A:ASP319 5.0 33.7 1.0

S.Duquerroy, C.Camus, J.Janin. X-Ray Structure and Catalytic Mechanism of Lobster Enolase. Biochemistry V. 34 12513 1995.
ISSN: ISSN 0006-2960
PubMed: 7547999
DOI: 10.1021/BI00039A005