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Magnesium in PDB 1tid: Crystal Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa: Poised For Phosphorylation Complex with Atp, Crystal Form I

Enzymatic activity of Crystal Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa: Poised For Phosphorylation Complex with Atp, Crystal Form I

All present enzymatic activity of Crystal Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa: Poised For Phosphorylation Complex with Atp, Crystal Form I:
2.7.1.37;

Protein crystallography data

The structure of Crystal Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa: Poised For Phosphorylation Complex with Atp, Crystal Form I, PDB code: 1tid was solved by S.Masuda, K.S.Murakami, S.Wang, C.A.Olson, J.Donigan, F.Leon, S.A.Darst, E.A.Campbell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.50
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 49.465, 49.465, 265.692, 90.00, 90.00, 90.00
R / Rfree (%) 23.5 / 26.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa: Poised For Phosphorylation Complex with Atp, Crystal Form I (pdb code 1tid). 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 Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa: Poised For Phosphorylation Complex with Atp, Crystal Form I, PDB code: 1tid:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1tid

Go back to Magnesium Binding Sites List in 1tid
Magnesium binding site 1 out of 2 in the Crystal Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa: Poised For Phosphorylation Complex with Atp, Crystal Form I


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa: Poised For Phosphorylation Complex with Atp, Crystal Form I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg300

b:18.7
occ:1.00
 OD1 A:ASN50 2.1 35.6 1.0
O A:HOH301 2.2 4.1 1.0
O1B A:ATP200 2.3 36.4 1.0
O1G A:ATP200 2.5 35.4 1.0
O A:HOH313 2.6 21.5 1.0
O1A A:ATP200 2.8 36.9 1.0
PA A:ATP200 3.1 37.7 1.0
O3A A:ATP200 3.1 35.9 1.0
CG A:ASN50 3.2 38.1 1.0
PB A:ATP200 3.2 34.9 1.0
PG A:ATP200 3.3 33.1 1.0
O3B A:ATP200 3.3 34.5 1.0
O2G A:ATP200 3.7 30.2 1.0
ND2 A:ASN50 3.8 39.9 1.0
CA A:GLY109 3.8 35.0 1.0
O A:HOH312 4.0 19.9 1.0
O5' A:ATP200 4.2 40.8 1.0
O2A A:ATP200 4.2 36.6 1.0
O A:GLU46 4.2 24.6 1.0
N A:GLY109 4.3 36.3 1.0
NE2 A:HIS54 4.3 47.1 1.0
OE1 A:GLU46 4.3 32.1 1.0
CB A:ASN50 4.4 38.6 1.0
CD2 A:HIS54 4.4 47.3 1.0
CA A:ASN50 4.5 39.2 1.0
O2B A:ATP200 4.6 34.9 1.0
O3G A:ATP200 4.6 34.8 1.0
N A:ASN50 4.8 37.7 1.0
NH2 A:ARG105 4.9 28.3 1.0
C A:GLY109 5.0 35.6 1.0

Magnesium binding site 2 out of 2 in 1tid

Go back to Magnesium Binding Sites List in 1tid
Magnesium binding site 2 out of 2 in the Crystal Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa: Poised For Phosphorylation Complex with Atp, Crystal Form I


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa: Poised For Phosphorylation Complex with Atp, Crystal Form I within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg301

b:39.2
occ:1.00
 OD1 C:ASN50 2.4 26.6 1.0
O1B C:ATP201 2.4 38.6 1.0
O1G C:ATP201 2.4 38.1 1.0
O2G C:ATP201 2.9 37.1 1.0
PG C:ATP201 3.0 37.4 1.0
O3B C:ATP201 3.3 36.5 1.0
PB C:ATP201 3.3 37.9 1.0
O1A C:ATP201 3.4 34.3 1.0
O3A C:ATP201 3.5 35.7 1.0
CG C:ASN50 3.5 29.0 1.0
PA C:ATP201 3.7 34.3 1.0
ND2 C:ASN50 4.1 26.9 1.0
OE1 C:GLU46 4.2 38.1 1.0
O C:GLU46 4.3 33.5 1.0
NH2 C:ARG105 4.4 22.7 1.0
O3G C:ATP201 4.4 38.8 1.0
NE2 C:HIS54 4.4 38.9 1.0
CA C:GLY109 4.5 33.8 1.0
CD1 C:ILE53 4.6 35.4 1.0
O2B C:ATP201 4.7 37.2 1.0
N C:GLY109 4.7 35.0 1.0
CB C:ASN50 4.7 29.7 1.0
CA C:ASN50 4.7 28.7 1.0
O5' C:ATP201 4.7 37.2 1.0
N C:ASN50 4.7 29.2 1.0
NE C:ARG105 4.8 26.6 1.0
O2A C:ATP201 4.8 32.7 1.0
CD2 C:HIS54 5.0 38.0 1.0

Reference:

S.Masuda, K.S.Murakami, S.Wang, C.A.Olson, J.Donigian, F.Leon, S.A.Darst, E.A.Campbell. Crystal Structures of the Adp and Atp Bound Forms of the Bacillus Anti-Sigma Factor Spoiiab in Complex with the Anti-Anti-Sigma Spoiiaa. J.Mol.Biol. V. 340 941 2004.
ISSN: ISSN 0022-2836
PubMed: 15236958
DOI: 10.1016/J.JMB.2004.05.040
Page generated: Sun Aug 10 04:53:32 2025

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