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Magnesium in PDB 2v55: Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure

Enzymatic activity of Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure

All present enzymatic activity of Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure:
2.7.11.1;

Protein crystallography data

The structure of Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure, PDB code: 2v55 was solved by D.Komander, R.Garg, P.T.C.Wan, A.J.Ridley, D.Barford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.288 / 3.7
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 152.477, 152.477, 531.274, 90.00, 90.00, 120.00
R / Rfree (%) 23.76 / 26.89

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure (pdb code 2v55). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure, PDB code: 2v55:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 2v55

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Magnesium binding site 1 out of 4 in the Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1481

b:0.8
occ:1.00
OD1 A:ASN203 2.9 77.4 1.0
N3B A:ANP1480 3.3 0.1 1.0
O1A A:ANP1480 3.3 0.5 1.0
C5' A:ANP1480 3.3 0.1 1.0
O3G A:ANP1480 3.3 0.7 1.0
O2B A:ANP1480 3.6 0.6 1.0
O3A A:ANP1480 3.7 0.3 1.0
PB A:ANP1480 3.7 0.6 1.0
PA A:ANP1480 3.8 0.7 1.0
O5' A:ANP1480 3.8 0.2 1.0
PG A:ANP1480 3.9 0.4 1.0
CG A:ASN203 3.9 76.8 1.0
OD2 A:ASP216 4.1 0.5 1.0
CE A:LYS200 4.1 65.6 1.0
CB A:ASP202 4.3 0.6 1.0
O A:ASP202 4.3 85.2 1.0
NZ A:LYS200 4.4 69.1 1.0
ND2 A:ASN203 4.4 80.1 1.0
C4' A:ANP1480 4.5 0.7 1.0
C A:ASP202 4.6 86.8 1.0
O3' A:ANP1480 4.7 0.4 1.0
C3' A:ANP1480 4.7 0.2 1.0
CG A:ASP216 4.8 0.3 1.0
CB A:ASP216 4.9 0.1 1.0
O2G A:ANP1480 4.9 0.8 1.0

Magnesium binding site 2 out of 4 in 2v55

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Magnesium binding site 2 out of 4 in the Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1202

b:50.3
occ:1.00
O2B B:GTP1201 2.4 49.9 1.0
OG1 B:THR37 2.5 48.7 1.0
O2G B:GTP1201 2.6 50.2 1.0
OG1 B:THR55 2.7 49.2 1.0
O B:VAL53 2.9 0.2 1.0
CB B:THR37 3.1 59.9 1.0
N B:THR55 3.2 82.9 1.0
CG2 B:THR55 3.4 49.1 1.0
PB B:GTP1201 3.4 55.8 1.0
CB B:THR55 3.4 71.6 1.0
PG B:GTP1201 3.6 73.4 1.0
O3A B:GTP1201 3.6 0.2 1.0
O1A B:GTP1201 3.6 51.5 1.0
CG2 B:THR37 3.8 63.2 1.0
O3G B:GTP1201 3.8 72.2 1.0
CA B:THR55 3.9 71.8 1.0
O3B B:GTP1201 3.9 93.9 1.0
C B:VAL53 4.0 84.1 1.0
PA B:GTP1201 4.1 69.9 1.0
C B:PRO54 4.2 78.7 1.0
CA B:PRO54 4.3 68.2 1.0
CE1 B:TYR52 4.3 81.4 1.0
CA B:THR37 4.5 57.3 1.0
O2A B:GTP1201 4.5 50.5 1.0
OD2 B:ASP77 4.5 85.6 1.0
N B:THR37 4.6 66.2 1.0
N B:PRO54 4.7 53.2 1.0
CD1 B:TYR52 4.7 85.1 1.0
O1B B:GTP1201 4.7 50.8 1.0
O1G B:GTP1201 4.9 82.2 1.0
N B:VAL53 5.0 74.9 1.0
CZ B:TYR52 5.0 68.0 1.0
C B:THR55 5.0 62.8 1.0

Magnesium binding site 3 out of 4 in 2v55

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Magnesium binding site 3 out of 4 in the Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1481

b:99.4
occ:1.00
OD1 C:ASN203 2.9 83.1 1.0
O1A C:ANP1480 3.2 0.7 1.0
N3B C:ANP1480 3.2 0.1 1.0
C5' C:ANP1480 3.3 0.2 1.0
O3G C:ANP1480 3.3 0.3 1.0
O2B C:ANP1480 3.6 1.0 1.0
O3A C:ANP1480 3.6 0.7 1.0
PB C:ANP1480 3.7 0.1 1.0
PA C:ANP1480 3.8 0.4 1.0
O5' C:ANP1480 3.8 0.1 1.0
PG C:ANP1480 3.9 0.2 1.0
CG C:ASN203 4.0 80.5 1.0
OD2 C:ASP216 4.0 0.1 1.0
CE C:LYS200 4.1 63.9 1.0
CB C:ASP202 4.3 0.4 1.0
O C:ASP202 4.4 83.7 1.0
NZ C:LYS200 4.4 62.7 1.0
ND2 C:ASN203 4.5 80.1 1.0
C4' C:ANP1480 4.5 0.6 1.0
C C:ASP202 4.6 86.9 1.0
C3' C:ANP1480 4.6 0.6 1.0
O3' C:ANP1480 4.7 0.8 1.0
CG C:ASP216 4.8 0.1 1.0
CB C:ASP216 4.9 0.2 1.0
O2G C:ANP1480 4.9 0.6 1.0

Magnesium binding site 4 out of 4 in 2v55

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Magnesium binding site 4 out of 4 in the Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1202

b:34.3
occ:1.00
OG1 D:THR55 2.6 31.7 1.0
OG1 D:THR37 2.6 53.4 1.0
O2B D:GTP1201 2.6 30.1 1.0
O2G D:GTP1201 2.7 41.0 1.0
O D:VAL53 2.9 0.4 1.0
CB D:THR37 3.1 65.0 1.0
N D:THR55 3.1 81.2 1.0
CG2 D:THR55 3.3 34.4 1.0
CB D:THR55 3.3 67.8 1.0
PB D:GTP1201 3.5 65.0 1.0
O1A D:GTP1201 3.7 38.2 1.0
O3A D:GTP1201 3.7 1.0 1.0
PG D:GTP1201 3.7 68.4 1.0
CG2 D:THR37 3.7 64.5 1.0
CA D:THR55 3.8 70.5 1.0
O3G D:GTP1201 3.9 73.4 1.0
C D:VAL53 4.0 83.8 1.0
O3B D:GTP1201 4.0 95.7 1.0
C D:PRO54 4.1 77.3 1.0
PA D:GTP1201 4.2 55.6 1.0
CA D:PRO54 4.3 63.4 1.0
CE1 D:TYR52 4.4 83.3 1.0
OD2 D:ASP77 4.4 84.2 1.0
CA D:THR37 4.5 56.7 1.0
O2A D:GTP1201 4.6 38.0 1.0
N D:PRO54 4.6 54.7 1.0
N D:THR37 4.7 66.8 1.0
CD1 D:TYR52 4.7 88.3 1.0
O1B D:GTP1201 4.9 43.8 1.0
C D:THR55 4.9 61.8 1.0
N D:VAL53 5.0 71.7 1.0

Reference:

D.Komander, R.Garg, P.T.C.Wan, A.J.Ridley, D.Barford. Mechanism of Multi-Site Phosphorylation From A Rock-I:Rhoe Complex Structure. Embo J. V. 27 3175 2008.
ISSN: ISSN 0261-4189
PubMed: 18946488
DOI: 10.1038/EMBOJ.2008.226
Page generated: Wed Aug 14 04:58:51 2024

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