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. Author manuscript; available in PMC: 2006 Jan 20.
Published in final edited form as: J Biol Chem. 2005 Oct 14;280(49):40668–40675. doi: 10.1074/jbc.M509748200

Table 1.

Comparisons of the active sites of human GLX2-2 and A. thaliana GLX2-5a

Metalb Enzyme Residue Atom Distance (Å) Bond angle (°)c Second Sphere ligands
M1 GLX2-5 His54 Nɛ2 2.1 119 Thr53
GLX2-2 His54 Nɛ2 2.3 104
M1 GLX2-5 His56 Nδ1 2.1 104
GLX2-2 His56 Nδ1 2.3 95 Glu146 via water
M1 GLX2-5 His112 Nɛ2 2.1 129 Lys140 carbonyl
GLX2-2 His110 Nɛ2 2.3 161
M1 GLX2-5 Bridging 2.0
GLX2-2 H2O/OH− 2.1
M1 GLX2-5 None
GLX2-2 Asp134 Oδ2 2.2 78 Asp134 carbonyl
M2 GLX2-5 Asp58 Oδ2 2.0 90
GLX2-2 Asp58 Oδ2 2.3 87
M2 GLX2-5 His59 Nɛ2 1.9 107 Asp29
GLX2-2 His59 Nɛ2 2.2 101
M2 GLX2-5 Asp131 Oδ2 2.0 81
GLX2-2 Asp134 Oδ2 2.2 78
M2 GLX2-5 His169 Nɛ2 1.9 141 Asp11
GLX2-2 His173 Nɛ2 2.1 151
M2 GLX2-5 Bridging 2.1
GLX2-2 H2O/OH− 2.1
a

Structures for human GLX2-2 (Protein Data Bank number: 1QH3) and A. thaliana GLX2-5 (Protein Data Bank number: 1XM8) were analyzed with Raswin v. 2.7.2.1.

b

M1 is Zn(II) for both enzymes; M2 is Zn(II) for human GLX2-2 and Fe for A. thaliana GLX2-5.

c

Bond angle is defined as the bridging H2O/OH− - metal – ligating atom of ligand.