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Magnesium in PDB 1s2v: Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II)

Enzymatic activity of Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II)

All present enzymatic activity of Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II):
5.4.2.9;

Protein crystallography data

The structure of Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II), PDB code: 1s2v was solved by S.Liu, Z.Lu, Y.Han, Y.Jia, A.Howard, D.Dunaway-Mariano, O.Herzberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.00 / 2.10
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 122.517, 86.469, 104.011, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 25.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II) (pdb code 1s2v). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II), PDB code: 1s2v:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1s2v

Go back to Magnesium Binding Sites List in 1s2v
Magnesium binding site 1 out of 4 in the Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1001

b:48.4
occ:1.00
O A:HOH1224 2.1 41.8 1.0
OD2 A:ASP85 2.2 37.2 1.0
O A:HOH1211 2.4 53.2 1.0
O A:HOH1007 2.7 35.5 1.0
O A:HOH1163 2.8 37.4 1.0
CG A:ASP85 2.9 33.7 1.0
OD1 A:ASP85 2.9 35.9 1.0
O A:HOH1114 2.9 40.9 1.0
NH1 A:ARG159 3.6 53.3 1.0
O A:HOH1048 3.9 43.5 1.0
OD2 A:ASP58 4.2 37.8 1.0
CB A:ASP85 4.3 32.0 1.0
OD1 A:ASP87 4.3 31.2 1.0
CA A:GLY47 4.4 29.2 1.0
N A:GLY47 4.5 27.2 1.0
OE1 A:GLU114 4.5 40.7 1.0
N A:LEU48 4.7 28.6 1.0
CZ A:ARG159 4.7 53.1 1.0
OD1 A:ASP58 4.8 38.4 1.0
O A:HOH1005 4.9 22.9 1.0
C A:GLY47 5.0 29.4 1.0
CG A:ASP58 5.0 36.3 1.0

Magnesium binding site 2 out of 4 in 1s2v

Go back to Magnesium Binding Sites List in 1s2v
Magnesium binding site 2 out of 4 in the Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1002

b:33.3
occ:0.50
O B:HOH1235 1.9 30.4 1.0
O B:HOH1234 2.1 40.2 1.0
O B:HOH1196 2.2 43.2 1.0
O B:HOH1236 2.2 37.8 1.0
OD2 B:ASP85 2.2 21.8 1.0
O B:HOH1238 2.4 60.4 1.0
CG B:ASP85 3.2 21.5 1.0
OD1 B:ASP85 3.5 20.4 1.0
OD2 B:ASP58 3.7 31.3 1.0
NH1 B:ARG159 3.8 46.2 1.0
O B:HOH1021 4.0 43.1 1.0
CA B:GLY47 4.1 21.0 1.0
N B:LEU48 4.2 23.1 1.0
N B:GLY47 4.2 20.8 1.0
OD1 B:ASP87 4.3 33.1 1.0
O B:HOH1004 4.4 20.0 1.0
OD1 B:ASP58 4.4 32.9 1.0
CG B:ASP58 4.4 31.2 1.0
C B:GLY47 4.5 23.4 1.0
CB B:ASP85 4.5 20.5 1.0
OE1 B:GLU114 4.6 35.1 1.0
O B:HOH1110 4.8 32.4 1.0
O B:HOH1220 4.8 52.5 1.0
CZ B:ARG159 4.8 45.0 1.0

Magnesium binding site 3 out of 4 in 1s2v

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Magnesium binding site 3 out of 4 in the Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1003

b:35.7
occ:1.00
O C:HOH1243 1.9 38.7 1.0
O C:HOH1242 2.0 32.1 1.0
O C:HOH1221 2.1 44.4 1.0
OD2 C:ASP85 2.2 26.0 1.0
O C:HOH1119 2.3 37.0 1.0
O C:HOH1193 2.8 63.0 1.0
CG C:ASP85 3.1 27.3 1.0
OD1 C:ASP85 3.3 28.7 1.0
OD2 C:ASP58 3.6 33.8 1.0
CA C:GLY47 3.9 25.2 1.0
OD1 C:ASP87 4.0 36.1 1.0
N C:LEU48 4.0 27.0 1.0
OD1 C:ASP58 4.1 27.7 1.0
N C:GLY47 4.2 27.1 1.0
O C:HOH1080 4.2 34.3 1.0
C C:GLY47 4.3 27.0 1.0
CG C:ASP58 4.3 29.6 1.0
O C:HOH1085 4.4 33.9 1.0
O C:HOH1016 4.5 34.5 1.0
CB C:ASP85 4.5 23.5 1.0
O C:HOH1075 4.7 39.0 1.0
CA C:LEU48 5.0 26.2 1.0
O C:HOH1089 5.0 42.2 1.0

Magnesium binding site 4 out of 4 in 1s2v

Go back to Magnesium Binding Sites List in 1s2v
Magnesium binding site 4 out of 4 in the Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Mg(II) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1004

b:37.4
occ:1.00
O D:HOH1228 2.1 35.2 1.0
O D:HOH1187 2.1 34.8 1.0
O D:HOH1065 2.2 38.4 1.0
OD2 D:ASP85 2.3 32.5 1.0
O D:HOH1189 2.4 38.5 1.0
O D:HOH1196 2.5 43.2 1.0
CG D:ASP85 3.1 29.4 1.0
OD1 D:ASP85 3.3 31.3 1.0
OD1 D:ASP87 3.7 29.9 1.0
OD2 D:ASP58 3.8 33.5 1.0
CA D:GLY47 4.1 23.3 1.0
O D:HOH1162 4.3 33.9 1.0
N D:GLY47 4.3 21.8 1.0
N D:LEU48 4.4 24.5 1.0
OD1 D:ASP58 4.5 32.5 1.0
CB D:ASP85 4.5 27.7 1.0
CG D:ASP58 4.6 31.4 1.0
OE1 D:GLU114 4.6 39.5 1.0
C D:GLY47 4.6 25.4 1.0
O D:HOH1010 4.7 21.8 1.0
O D:HOH1124 4.9 40.4 1.0
CG D:ASP87 4.9 29.9 1.0
OE2 D:GLU114 5.0 39.3 1.0

Reference:

S.Liu, Z.Lu, Y.Han, Y.Jia, A.Howard, D.Dunaway-Mariano, O.Herzberg. Conformational Flexibility of Pep Mutase Biochemistry V. 43 4447 2004.
ISSN: ISSN 0006-2960
PubMed: 15078090
DOI: 10.1021/BI036255H
Page generated: Tue Aug 13 13:14:40 2024

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