Magnesium in PDB 1a05: Crystal Structure of the Complex of 3-Isopropylmalate Dehydrogenase From Thiobacillus Ferrooxidans with 3- Isopropylmalate

All present enzymatic activity of Crystal Structure of the Complex of 3-Isopropylmalate Dehydrogenase From Thiobacillus Ferrooxidans with 3- Isopropylmalate:
1.1.1.85;

The structure of Crystal Structure of the Complex of 3-Isopropylmalate Dehydrogenase From Thiobacillus Ferrooxidans with 3- Isopropylmalate, PDB code: 1a05 was solved by K.Imada, K.Inagaki, H.Matsunami, H.Kawaguchi, H.Tanaka, N.Tanaka, K.Namba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	56.540, 114.240, 130.890, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 27.5

The binding sites of Magnesium atom in the Crystal Structure of the Complex of 3-Isopropylmalate Dehydrogenase From Thiobacillus Ferrooxidans with 3- Isopropylmalate (pdb code 1a05). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Complex of 3-Isopropylmalate Dehydrogenase From Thiobacillus Ferrooxidans with 3- Isopropylmalate, PDB code: 1a05:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Complex of 3-Isopropylmalate Dehydrogenase From Thiobacillus Ferrooxidans with 3- Isopropylmalate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Complex of 3-Isopropylmalate Dehydrogenase From Thiobacillus Ferrooxidans with 3- Isopropylmalate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:20.6 occ:1.00 O A:HOH562 2.3 16.6 1.0 O3 A:IPM401 2.3 19.1 1.0 O A:HOH602 2.4 23.9 1.0 OD1 A:ASP246 2.4 13.0 1.0 OD2 B:ASP222 2.4 22.0 1.0 O1 A:IPM401 2.4 17.0 1.0 C1 A:IPM401 3.0 17.8 1.0 C2 A:IPM401 3.2 12.2 1.0 CG B:ASP222 3.5 15.2 1.0 CG A:ASP246 3.5 15.8 1.0 OD1 A:ASP250 3.7 25.4 1.0 CB B:ASP222 3.8 15.0 1.0 O A:HOH553 3.9 7.5 1.0 OD2 A:ASP246 3.9 13.7 1.0 O A:HOH585 4.0 17.5 1.0 OD2 A:ASP250 4.1 19.2 1.0 CG A:ASP250 4.1 19.0 1.0 O2 A:IPM401 4.1 19.5 1.0 O A:ASP246 4.2 8.4 1.0 NH1 A:ARG105 4.3 13.3 1.0 NZ B:LYS190 4.4 14.0 1.0 C3 A:IPM401 4.4 15.1 1.0 C4 A:IPM401 4.4 16.3 1.0 O B:HOH432 4.5 13.8 1.0 O4 A:IPM401 4.5 13.2 1.0 OD1 B:ASP222 4.6 16.2 1.0 CB A:ASP246 4.7 12.1 1.0 CA A:ASP246 4.8 12.4 1.0 C A:ASP246 4.8 13.6 1.0 NH1 A:ARG133 4.8 12.6 1.0 O5 A:IPM401 4.9 17.9 1.0 NH2 A:ARG105 4.9 10.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Complex of 3-Isopropylmalate Dehydrogenase From Thiobacillus Ferrooxidans with 3- Isopropylmalate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Complex of 3-Isopropylmalate Dehydrogenase From Thiobacillus Ferrooxidans with 3- Isopropylmalate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:14.7 occ:1.00 OD1 B:ASP246 2.4 15.2 1.0 O2 B:IPM402 2.4 13.1 1.0 O B:HOH419 2.4 11.0 1.0 O A:HOH532 2.4 24.0 1.0 OD2 A:ASP222 2.4 21.9 1.0 O1 B:IPM402 2.6 22.9 1.0 C1 B:IPM402 3.2 19.4 1.0 C2 B:IPM402 3.4 14.6 1.0 CG B:ASP246 3.4 11.8 1.0 CG A:ASP222 3.4 15.6 1.0 CB A:ASP222 3.7 13.7 1.0 OD2 B:ASP246 3.9 8.9 1.0 O B:ASP246 4.0 12.8 1.0 O4 B:IPM402 4.1 14.7 1.0 OD1 B:ASP250 4.1 18.2 1.0 NZ A:LYS190 4.1 5.4 1.0 C4 B:IPM402 4.2 16.1 1.0 OD2 B:ASP250 4.2 14.9 1.0 O B:HOH441 4.3 11.6 1.0 CG B:ASP250 4.3 16.3 1.0 O B:HOH436 4.3 21.5 1.0 C3 B:IPM402 4.4 14.5 1.0 O3 B:IPM402 4.4 18.6 1.0 NH1 B:ARG105 4.5 26.8 1.0 CB B:ASP246 4.5 7.4 1.0 OD1 A:ASP222 4.6 21.1 1.0 O5 B:IPM402 4.6 13.6 1.0 C B:ASP246 4.6 14.2 1.0 CA B:ASP246 4.6 10.5 1.0 NH1 B:ARG133 4.6 9.1 1.0 O A:HOH522 4.7 10.9 1.0

K.Imada, K.Inagaki, H.Matsunami, H.Kawaguchi, H.Tanaka, N.Tanaka, K.Namba. Structure of 3-Isopropylmalate Dehydrogenase in Complex with 3-Isopropylmalate at 2.0 A Resolution: the Role of GLU88 in the Unique Substrate-Recognition Mechanism. Structure V. 6 971 1998.
ISSN: ISSN 0969-2126
PubMed: 9739088
DOI: 10.1016/S0969-2126(98)00099-9