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Magnesium in PDB 2vhq: P4 Protein From Bacteriophage PHI12 S252A Mutant in Complex with Atp and Mg

Protein crystallography data

The structure of P4 Protein From Bacteriophage PHI12 S252A Mutant in Complex with Atp and Mg, PDB code: 2vhq was solved by D.E.Kainov, E.J.Mancini, J.Telenius, J.Lisal, J.M.Grimes, D.H.Bamford, D.I.Stuart, R.Tuma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.50 / 2.15
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 105.244, 129.387, 158.978, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 24.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the P4 Protein From Bacteriophage PHI12 S252A Mutant in Complex with Atp and Mg (pdb code 2vhq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the P4 Protein From Bacteriophage PHI12 S252A Mutant in Complex with Atp and Mg, PDB code: 2vhq:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 2vhq

Go back to Magnesium Binding Sites List in 2vhq
Magnesium binding site 1 out of 3 in the P4 Protein From Bacteriophage PHI12 S252A Mutant in Complex with Atp and Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of P4 Protein From Bacteriophage PHI12 S252A Mutant in Complex with Atp and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1328

b:59.6
occ:1.00
O2A A:ATP1327 1.8 52.4 1.0
O1G A:ATP1327 2.1 62.9 1.0
O2B A:ATP1327 2.3 56.6 1.0
OG1 A:THR137 2.4 39.1 1.0
PA A:ATP1327 2.8 54.9 1.0
PB A:ATP1327 2.9 57.4 1.0
O3B A:ATP1327 2.9 60.8 1.0
PG A:ATP1327 2.9 64.2 1.0
O3A A:ATP1327 3.0 56.1 1.0
CB A:THR137 3.5 37.8 1.0
O3G A:ATP1327 3.6 63.2 1.0
O5' A:ATP1327 3.6 54.2 1.0
O A:HOH2198 3.9 41.6 1.0
O1A A:ATP1327 4.1 56.1 1.0
N A:THR137 4.2 38.4 1.0
O2G A:ATP1327 4.2 62.4 1.0
O1B A:ATP1327 4.3 56.6 1.0
CA A:THR137 4.4 37.8 1.0
O A:HOH2143 4.5 39.0 1.0
CG2 A:THR137 4.6 38.0 1.0
O A:HOH2199 4.6 52.4 1.0
OD1 A:ASP189 4.6 40.8 1.0
OD2 A:ASP189 4.8 42.2 1.0
OD1 A:ASN234 4.9 62.4 1.0
C5' A:ATP1327 5.0 54.3 1.0

Magnesium binding site 2 out of 3 in 2vhq

Go back to Magnesium Binding Sites List in 2vhq
Magnesium binding site 2 out of 3 in the P4 Protein From Bacteriophage PHI12 S252A Mutant in Complex with Atp and Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of P4 Protein From Bacteriophage PHI12 S252A Mutant in Complex with Atp and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1328

b:60.9
occ:1.00
O2A B:ATP1327 2.0 53.5 1.0
O1G B:ATP1327 2.3 61.6 1.0
O2B B:ATP1327 2.4 54.1 1.0
OG1 B:THR137 2.5 38.1 1.0
O3B B:ATP1327 2.8 60.1 1.0
PG B:ATP1327 2.9 62.5 1.0
PB B:ATP1327 3.0 55.9 1.0
PA B:ATP1327 3.2 53.8 1.0
O3G B:ATP1327 3.3 62.5 1.0
O3A B:ATP1327 3.4 54.5 1.0
CB B:THR137 3.6 36.4 1.0
O5' B:ATP1327 3.9 54.5 1.0
O B:HOH2200 4.1 41.4 1.0
N B:THR137 4.2 37.3 1.0
OD1 B:ASP189 4.3 42.2 1.0
O B:HOH2201 4.3 45.7 1.0
O2G B:ATP1327 4.3 60.8 1.0
O B:HOH2150 4.3 41.7 1.0
CA B:THR137 4.4 36.5 1.0
O1A B:ATP1327 4.4 56.2 1.0
O1B B:ATP1327 4.5 55.6 1.0
NH2 A:ARG272 4.6 46.1 1.0
CG2 B:THR137 4.7 36.9 1.0
OD2 B:ASP189 4.8 40.5 1.0
OG B:SER232 4.9 38.5 1.0
CG B:ASP189 5.0 35.5 1.0
OE2 B:GLU160 5.0 40.8 1.0

Magnesium binding site 3 out of 3 in 2vhq

Go back to Magnesium Binding Sites List in 2vhq
Magnesium binding site 3 out of 3 in the P4 Protein From Bacteriophage PHI12 S252A Mutant in Complex with Atp and Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of P4 Protein From Bacteriophage PHI12 S252A Mutant in Complex with Atp and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1328

b:61.5
occ:1.00
O2A C:ATP1327 1.9 51.4 1.0
O3G C:ATP1327 2.0 62.8 1.0
O2B C:ATP1327 2.5 54.5 1.0
OG1 C:THR137 2.7 38.6 1.0
PG C:ATP1327 2.8 62.8 1.0
O3B C:ATP1327 3.0 59.5 1.0
PB C:ATP1327 3.1 55.1 1.0
PA C:ATP1327 3.1 50.1 1.0
O2G C:ATP1327 3.4 62.1 1.0
O3A C:ATP1327 3.4 53.8 1.0
O C:HOH2189 3.8 35.9 1.0
CB C:THR137 3.9 37.0 1.0
O5' C:ATP1327 4.1 53.3 1.0
NH2 B:ARG272 4.2 46.0 1.0
O1G C:ATP1327 4.2 62.5 1.0
O1A C:ATP1327 4.2 54.4 1.0
O C:HOH2186 4.2 52.5 1.0
O C:HOH2125 4.3 30.8 1.0
OD1 C:ASP189 4.3 40.5 1.0
N C:THR137 4.4 37.4 1.0
O1B C:ATP1327 4.5 54.7 1.0
CA C:THR137 4.7 37.0 1.0
OD2 C:ASP189 4.8 40.8 1.0
OE1 C:GLU160 4.8 39.1 1.0
NH2 B:ARG279 4.8 54.3 1.0
CG2 C:THR137 4.9 37.8 1.0
CD C:GLU160 5.0 37.0 1.0

Reference:

D.E.Kainov, E.J.Mancini, J.Telenius, J.Lisal, J.M.Grimes, D.H.Bamford, D.I.Stuart, R.Tuma. Structural Basis of Mechanochemical Coupling in A Hexameric Molecular Motor. J.Biol.Chem. V. 283 3607 2008.
ISSN: ISSN 0021-9258
PubMed: 18057007
DOI: 10.1074/JBC.M706366200
Page generated: Wed Aug 14 05:12:52 2024

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