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Zinc in PDB 1o7d: The Structure of the Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low pH Activation

Enzymatic activity of The Structure of the Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low pH Activation

All present enzymatic activity of The Structure of the Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low pH Activation:
3.2.1.24;

Protein crystallography data

The structure of The Structure of the Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low pH Activation, PDB code: 1o7d was solved by P.Heikinheimo, R.Helland, H.S.Leiros, I.Leiros, S.Karlsen, G.Evjen, R.Ravelli, G.Schoehn, R.Ruigrok, O.-K.Tollersrud, S.Mcsweeney, E.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.70
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 117.880, 117.880, 582.040, 90.00, 90.00, 120.00
R / Rfree (%) 25.7 / 28.9

Zinc Binding Sites:

The binding sites of Zinc atom in the The Structure of the Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low pH Activation (pdb code 1o7d). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Structure of the Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low pH Activation, PDB code: 1o7d:

Zinc binding site 1 out of 1 in 1o7d

Go back to Zinc Binding Sites List in 1o7d
Zinc binding site 1 out of 1 in the The Structure of the Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low pH Activation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of the Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low pH Activation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn3

b:35.9
occ:1.00
 OD1 A:ASP74 2.1 27.1 1.0
NE2 A:HIS72 2.1 36.2 1.0
NE2 C:HIS446 2.2 38.0 1.0
O3 A:TRS2 2.3 35.7 1.0
OD2 A:ASP196 2.7 47.0 1.0
CG A:ASP74 2.9 27.1 1.0
N A:TRS2 3.0 35.7 1.0
CD2 A:HIS72 3.0 36.2 1.0
OD2 A:ASP74 3.1 27.1 1.0
CD2 C:HIS446 3.2 38.0 1.0
CE1 A:HIS72 3.2 36.2 1.0
CE1 C:HIS446 3.2 38.0 1.0
C3 A:TRS2 3.2 35.7 1.0
CG A:ASP196 3.3 47.0 1.0
CB A:ASP196 3.5 47.0 1.0
C A:TRS2 3.7 35.7 1.0
CG A:HIS72 4.2 36.2 1.0
ND1 A:HIS72 4.2 36.2 1.0
OD2 C:ASP447 4.2 54.0 1.0
OD1 A:ASP196 4.3 47.0 1.0
CG C:HIS446 4.3 38.0 1.0
CB A:ASP74 4.3 27.1 1.0
ND1 C:HIS446 4.3 38.0 1.0
C2 A:TRS2 4.5 35.7 1.0
OD1 A:ASP319 4.6 49.4 1.0
OH A:TYR261 4.8 26.7 1.0
OD1 C:ASP447 4.8 54.0 1.0
CG C:ASP447 4.9 54.0 1.0
C1 A:TRS2 4.9 35.7 1.0

Reference:

P.Heikinheimo, R.Helland, H.S.Leiros, I.Leiros, S.Karlsen, G.Evjen, R.Ravelli, G.Schoehn, R.Ruigrok, O.-K.Tollersrud, S.Mcsweeney, E.Hough. The Structure of Bovine Lysosomal Alpha-Mannosidase Suggests A Novel Mechanism For Low-pH Activation J.Mol.Biol. V. 327 631 2003.
ISSN: ISSN 0022-2836
PubMed: 12634058
DOI: 10.1016/S0022-2836(03)00172-4
Page generated: Wed Oct 16 17:28:13 2024

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