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Magnesium in PDB 1til: 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 II

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 II

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 II:
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 II, PDB code: 1til 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 / 2.70
Space group P 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 115.133, 115.133, 256.820, 90.00, 90.00, 90.00
R / Rfree (%) 23.4 / 26.5

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 II (pdb code 1til). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 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 II, PDB code: 1til:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1til

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Magnesium binding site 1 out of 3 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 II


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 II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg300

b:47.0
occ:1.00
OD1 A:ASN50 2.1 31.3 1.0
O2G A:ATP200 2.3 54.0 1.0
CG A:ASN50 2.8 28.8 1.0
O1A A:ATP200 2.9 36.1 1.0
O1B A:ATP200 3.0 41.5 1.0
ND2 A:ASN50 3.1 28.9 1.0
PA A:ATP200 3.5 36.4 1.0
OE1 A:GLU46 3.5 40.6 1.0
PG A:ATP200 3.6 53.5 1.0
O A:GLU46 3.7 30.1 1.0
O3A A:ATP200 3.7 40.3 1.0
O3B A:ATP200 3.8 45.2 1.0
CA A:GLY109 3.8 30.9 1.0
PB A:ATP200 3.9 41.0 1.0
O A:HOH313 4.0 37.7 1.0
CB A:ASN50 4.2 28.1 1.0
NH1 A:ARG105 4.2 40.0 1.0
N A:GLY109 4.5 31.0 1.0
CA A:ASN50 4.5 29.4 1.0
O2A A:ATP200 4.5 35.9 1.0
N A:ASN50 4.5 30.3 1.0
C A:GLU46 4.5 29.6 1.0
O5' A:ATP200 4.6 36.8 1.0
O1G A:ATP200 4.6 52.9 1.0
O3G A:ATP200 4.6 53.5 1.0
CA A:GLU46 4.7 30.0 1.0
CD A:GLU46 4.8 39.8 1.0
CB A:GLU46 4.8 31.2 1.0
C A:GLY109 4.9 30.6 1.0
CD2 A:HIS54 5.0 33.6 1.0

Magnesium binding site 2 out of 3 in 1til

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Magnesium binding site 2 out of 3 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 II


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 II within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg301

b:23.1
occ:1.00
O2G C:ATP201 2.0 49.2 1.0
OD1 C:ASN50 2.2 29.5 1.0
O1A C:ATP201 2.7 33.4 1.0
O1B C:ATP201 2.9 41.8 1.0
CG C:ASN50 3.2 27.8 1.0
PA C:ATP201 3.2 33.0 1.0
OE1 C:GLU46 3.3 46.4 1.0
PG C:ATP201 3.3 47.6 1.0
O3B C:ATP201 3.5 42.4 1.0
O3A C:ATP201 3.5 35.6 1.0
ND2 C:ASN50 3.6 27.6 1.0
PB C:ATP201 3.7 38.8 1.0
CA C:GLY109 3.7 33.3 1.0
O C:GLU46 3.9 34.6 1.0
O D:HOH125 4.1 41.1 1.0
O2A C:ATP201 4.2 34.7 1.0
O3G C:ATP201 4.2 45.3 1.0
N C:GLY109 4.3 32.5 1.0
O5' C:ATP201 4.3 31.5 1.0
O1G C:ATP201 4.3 48.0 1.0
CD C:GLU46 4.5 44.6 1.0
NH1 C:ARG105 4.5 35.7 1.0
CB C:ASN50 4.5 27.9 1.0
C C:GLY109 4.7 33.9 1.0
CA C:ASN50 4.8 27.3 1.0
N C:ASN50 4.8 27.5 1.0
C C:GLU46 4.8 32.8 1.0
NE2 C:HIS54 4.8 23.0 1.0
CD2 C:HIS54 4.9 22.4 1.0

Magnesium binding site 3 out of 3 in 1til

Go back to Magnesium Binding Sites List in 1til
Magnesium binding site 3 out of 3 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 II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 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 II within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg302

b:35.8
occ:1.00
OD1 E:ASN50 2.1 42.1 1.0
O2G E:ATP202 2.4 57.2 1.0
O1A E:ATP202 2.8 46.6 1.0
O1B E:ATP202 2.9 52.0 1.0
CG E:ASN50 2.9 41.4 1.0
ND2 E:ASN50 3.3 42.1 1.0
OE1 E:GLU46 3.3 48.3 1.0
PA E:ATP202 3.3 46.0 1.0
O3B E:ATP202 3.3 52.2 1.0
CA E:GLY109 3.3 39.3 1.0
O3A E:ATP202 3.5 46.0 1.0
PG E:ATP202 3.5 56.5 1.0
PB E:ATP202 3.5 48.1 1.0
O E:GLU46 4.0 43.2 1.0
N E:GLY109 4.0 39.5 1.0
O E:HOH307 4.1 27.1 1.0
O1G E:ATP202 4.3 56.2 1.0
O2A E:ATP202 4.3 47.5 1.0
CB E:ASN50 4.3 38.3 1.0
O5' E:ATP202 4.4 47.7 1.0
C E:GLY109 4.4 39.5 1.0
NH1 E:ARG105 4.5 41.6 1.0
CD E:GLU46 4.5 46.8 1.0
CA E:ASN50 4.6 37.5 1.0
O3G E:ATP202 4.6 54.5 1.0
N E:ASN50 4.7 37.4 1.0
C E:GLU46 4.8 42.5 1.0
N E:PHE110 4.8 38.4 1.0
NE2 E:HIS54 4.9 39.6 1.0
CD2 E:HIS54 5.0 40.6 1.0
CA E:GLU46 5.0 42.6 1.0
O2B E:ATP202 5.0 48.3 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 04:53:40 2025

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