Manganese in PDB 2hxg: Crystal Structure of MN2+ Bound Ecai

All present enzymatic activity of Crystal Structure of MN2+ Bound Ecai:
5.3.1.4;

The structure of Crystal Structure of MN2+ Bound Ecai, PDB code: 2hxg was solved by B.A.Manjasetty, S.K.Burley, New York Sgx Research Center For Structuralgenomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	116.870, 116.870, 215.076, 90.00, 90.00, 120.00
R / Rfree (%)	22.9 / 28.8

The binding sites of Manganese atom in the Crystal Structure of MN2+ Bound Ecai (pdb code 2hxg). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Crystal Structure of MN2+ Bound Ecai, PDB code: 2hxg:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Crystal Structure of MN2+ Bound Ecai


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of MN2+ Bound Ecai within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:35.4 occ:1.00 OE1 A:GLU306 1.9 56.3 1.0 NE2 A:HIS350 2.2 43.7 1.0 NE2 A:HIS450 2.4 47.3 1.0 OE2 A:GLU333 2.4 54.5 1.0 O A:HOH504 2.5 10.5 1.0 O A:HOH503 2.7 24.6 1.0 CD A:GLU333 3.0 52.4 1.0 CD2 A:HIS350 3.0 45.0 1.0 CD A:GLU306 3.2 54.1 1.0 OE1 A:GLU333 3.2 56.1 1.0 CE1 A:HIS350 3.3 44.0 1.0 CD2 A:HIS450 3.3 48.2 1.0 CE1 A:HIS450 3.5 46.5 1.0 OE2 A:GLU306 3.8 53.7 1.0 CG A:GLU333 4.2 51.9 1.0 CE1 A:HIS449 4.2 49.5 1.0 CG A:HIS350 4.2 45.8 1.0 ND1 A:HIS449 4.3 50.4 1.0 CG A:GLU306 4.3 53.3 1.0 ND1 A:HIS350 4.3 44.0 1.0 CG A:HIS450 4.5 48.8 1.0 ND1 A:HIS450 4.6 46.3 1.0 CB A:GLU333 4.6 51.0 1.0 CZ A:PHE331 4.9 48.2 1.0

Manganese binding site 2 out of 3 in the Crystal Structure of MN2+ Bound Ecai


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of MN2+ Bound Ecai within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn501 b:50.2 occ:1.00 OE1 B:GLU306 2.0 46.9 1.0 NE2 B:HIS350 2.1 43.8 1.0 OE2 B:GLU333 2.2 41.5 1.0 O B:HOH504 2.5 28.2 1.0 CE1 B:HIS350 2.8 44.9 1.0 O B:HOH533 2.8 22.0 1.0 NE2 B:HIS450 2.8 48.7 1.0 CD B:GLU333 2.9 44.2 1.0 CD B:GLU306 3.0 47.0 1.0 CD2 B:HIS350 3.0 44.6 1.0 OE1 B:GLU333 3.1 42.4 1.0 OE2 B:GLU306 3.6 49.2 1.0 CD2 B:HIS450 3.6 48.1 1.0 ND1 B:HIS350 3.8 44.3 1.0 CE1 B:HIS450 3.9 48.9 1.0 CG B:HIS350 3.9 44.8 1.0 CG B:GLU306 4.1 46.2 1.0 CG B:GLU333 4.2 44.7 1.0 ND1 B:HIS449 4.6 49.4 1.0 CB B:GLU333 4.6 44.8 1.0 CE1 B:HIS449 4.7 48.6 1.0 CG B:HIS450 4.9 48.2 1.0 CZ B:PHE331 4.9 42.5 1.0 ND1 B:HIS450 4.9 49.0 1.0

Manganese binding site 3 out of 3 in the Crystal Structure of MN2+ Bound Ecai


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of MN2+ Bound Ecai within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn501 b:71.7 occ:1.00 O C:HOH508 2.4 88.8 1.0 OE2 C:GLU333 2.4 39.4 1.0 O C:HOH503 2.5 45.6 1.0 OE1 C:GLU306 2.5 43.9 1.0 NE2 C:HIS450 2.7 49.4 1.0 NE2 C:HIS350 3.0 43.8 1.0 OE2 C:GLU306 3.2 44.4 1.0 CD C:GLU306 3.2 44.7 1.0 CE1 C:HIS450 3.5 49.3 1.0 CD C:GLU333 3.5 41.1 1.0 O C:HOH504 3.6 48.6 1.0 CD2 C:HIS350 3.7 43.8 1.0 OE1 C:GLU333 3.8 39.6 1.0 CD2 C:HIS450 3.9 49.0 1.0 NE2 C:HIS449 3.9 48.0 1.0 CE1 C:HIS350 4.0 44.0 1.0 CD2 C:HIS449 4.5 47.9 1.0 ND1 C:HIS450 4.7 49.1 1.0 CA C:GLY305 4.7 45.6 1.0 CG C:GLU306 4.7 45.2 1.0 CG C:GLU333 4.8 41.5 1.0 N C:GLU306 4.8 45.5 1.0 CG C:HIS350 4.8 44.2 1.0 CE C:MET185 4.9 46.3 1.0 CG C:HIS450 4.9 48.9 1.0 ND1 C:HIS350 5.0 44.2 1.0 CE1 C:HIS449 5.0 48.0 1.0

W.Zhu, M.R.Chance, B.A.Manjasetty. Crystal Structure of MN2+-Bound Escherichia Coli L-Arabinose Isomerase (Ecai) and Implications in Protein Catalytic Mechanism and Thermo-Stability. J.Young.Investig. V. 17 2007.
ISSN: ESSN 1539-4026