Magnesium in PDB 3qml: The Structural Analysis of SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Novel Nucleotide Exchange Factor

The structure of The Structural Analysis of SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Novel Nucleotide Exchange Factor, PDB code: 3qml was solved by M.Yan, J.Z.Li, B.D.Sha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.13 / 2.31
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	226.353, 116.586, 55.844, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 27.1

The binding sites of Magnesium atom in the The Structural Analysis of SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Novel Nucleotide Exchange Factor (pdb code 3qml). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the The Structural Analysis of SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Novel Nucleotide Exchange Factor, PDB code: 3qml:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the The Structural Analysis of SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Novel Nucleotide Exchange Factor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structural Analysis of SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Novel Nucleotide Exchange Factor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1 b:62.5 occ:1.00 O A:HOH477 2.5 54.8 1.0 NZ A:LYS288 3.7 50.3 1.0 NH2 A:ARG284 4.0 60.3 1.0 CE A:LYS288 4.8 47.2 1.0 CD A:LYS288 4.8 47.4 1.0

Magnesium binding site 2 out of 3 in the The Structural Analysis of SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Novel Nucleotide Exchange Factor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structural Analysis of SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Novel Nucleotide Exchange Factor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg427 b:64.0 occ:1.00 CE A:LYS68 3.5 79.6 1.0 ND2 A:ASN69 3.7 66.4 1.0 NZ A:LYS68 4.0 71.4 1.0 OD1 A:ASN69 4.5 76.0 1.0 CG A:ASN69 4.5 74.0 1.0 CD A:LYS68 4.6 80.2 1.0 CG A:LYS68 4.9 74.1 1.0

Magnesium binding site 3 out of 3 in the The Structural Analysis of SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Novel Nucleotide Exchange Factor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of The Structural Analysis of SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Novel Nucleotide Exchange Factor within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg1 b:58.9 occ:1.00 CD C:LYS363 3.0 98.3 1.0 CE C:LYS363 3.4 96.5 1.0 CG C:LYS363 3.4 89.4 1.0 NZ C:LYS363 3.6 90.2 1.0 N C:LYS363 3.8 45.7 1.0 CB C:LYS363 3.9 75.6 1.0 OD1 C:ASN362 4.3 87.0 1.0 CB C:ASN362 4.3 62.1 1.0 CA C:LYS363 4.5 55.3 1.0 CA C:ASN362 4.6 40.9 1.0 CG C:ASN362 4.6 79.0 1.0 C C:ASN362 4.8 40.8 1.0

M.Yan, J.Li, B.Sha. Structural Analysis of the SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Nucleotide-Exchange Factor. Biochem.J. V. 438 447 2011.
ISSN: ISSN 0264-6021
PubMed: 21675960
DOI: 10.1042/BJ20110500