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Magnesium in PDB 1igw: Crystal Structure of the Isocitrate Lyase From the A219C Mutant of Escherichia Coli

Enzymatic activity of Crystal Structure of the Isocitrate Lyase From the A219C Mutant of Escherichia Coli

All present enzymatic activity of Crystal Structure of the Isocitrate Lyase From the A219C Mutant of Escherichia Coli:
4.1.3.1;

Protein crystallography data

The structure of Crystal Structure of the Isocitrate Lyase From the A219C Mutant of Escherichia Coli, PDB code: 1igw was solved by K.L.Britton, I.S.B.Abeysinghe, P.J.Baker, V.Barynin, P.Diehl, S.J.Langridge, B.A.Mcfadden, S.E.Sedelnikova, T.J.Stillman, K.Weeradechapon, D.W.Rice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.10
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 88.650, 88.650, 199.400, 90.00, 90.00, 120.00
R / Rfree (%) 18.4 / 23.5

Other elements in 1igw:

The structure of Crystal Structure of the Isocitrate Lyase From the A219C Mutant of Escherichia Coli also contains other interesting chemical elements:

Mercury (Hg) 21 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Isocitrate Lyase From the A219C Mutant of Escherichia Coli (pdb code 1igw). 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 the Isocitrate Lyase From the A219C Mutant of Escherichia Coli, PDB code: 1igw:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1igw

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Magnesium binding site 1 out of 4 in the Crystal Structure of the Isocitrate Lyase From the A219C Mutant of Escherichia Coli


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 the Isocitrate Lyase From the A219C Mutant of Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg441

b:26.4
occ:1.00
 O A:HOH1630 2.0 14.7 1.0
O1 A:PYR1444 2.0 27.5 1.0
OD2 A:ASP157 2.1 12.4 1.0
O A:HOH1631 2.1 18.3 1.0
O A:HOH1632 2.2 18.2 1.0
O3 A:PYR1444 2.3 20.0 1.0
C1 A:PYR1444 2.9 30.6 1.0
CG A:ASP157 3.1 13.1 1.0
C2 A:PYR1444 3.1 25.1 1.0
OD1 A:ASP157 3.3 15.6 1.0
O2 A:PYR1444 4.1 21.6 1.0
OD1 A:ASP108 4.2 30.0 1.0
CG A:GLU159 4.2 26.4 1.0
OD2 A:ASP108 4.2 31.7 1.0
OE2 A:GLU186 4.3 22.8 1.0
N A:TRP93 4.3 22.1 1.0
NH1 A:ARG232 4.3 25.5 1.0
OE2 A:GLU159 4.3 18.8 1.0
N A:GLY92 4.3 22.6 1.0
CA A:GLY92 4.4 20.8 1.0
CB A:ASP157 4.4 13.5 1.0
C3 A:PYR1444 4.4 34.7 1.0
CE1 A:HIS184 4.5 13.6 1.0
O A:HOH1550 4.6 33.6 1.0
CD A:GLU159 4.6 22.7 1.0
CG A:ASP108 4.7 27.9 1.0
C A:GLY92 4.7 21.6 1.0
O A:HOH1544 4.9 36.7 1.0

Magnesium binding site 2 out of 4 in 1igw

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Magnesium binding site 2 out of 4 in the Crystal Structure of the Isocitrate Lyase From the A219C Mutant of Escherichia Coli


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 the Isocitrate Lyase From the A219C Mutant of Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg441

b:18.5
occ:1.00
 O B:HOH1633 2.1 11.6 1.0
O B:HOH1635 2.1 19.5 1.0
OD2 B:ASP157 2.1 14.2 1.0
O3 B:PYR1445 2.2 17.4 1.0
O B:HOH1634 2.2 16.8 1.0
O1 B:PYR1445 2.3 14.7 1.0
C2 B:PYR1445 2.5 17.0 1.0
C1 B:PYR1445 2.8 16.6 1.0
CG B:ASP157 3.2 15.6 1.0
OD1 B:ASP157 3.6 15.3 1.0
O B:HOH1524 3.8 26.2 1.0
C3 B:PYR1445 3.9 7.0 1.0
O2 B:PYR1445 4.0 10.3 1.0
NH1 B:ARG232 4.0 18.4 1.0
N B:GLY92 4.1 13.9 1.0
OD2 B:ASP108 4.2 19.6 1.0
CA B:GLY92 4.2 12.1 1.0
N B:TRP93 4.2 10.5 1.0
OD1 B:ASP108 4.2 20.0 1.0
O B:HOH1610 4.4 39.4 1.0
CB B:ASP157 4.5 16.4 1.0
OE2 B:GLU159 4.5 28.8 1.0
CE1 B:HIS184 4.5 19.6 1.0
OE2 B:GLU186 4.5 13.3 1.0
C B:GLY92 4.6 12.0 1.0
CG B:ASP108 4.6 15.5 1.0
CD B:GLU159 4.8 31.6 1.0
CG B:GLU159 4.8 31.0 1.0
OH B:TYR89 4.9 18.0 1.0
CZ B:ARG232 5.0 22.1 1.0

Magnesium binding site 3 out of 4 in 1igw

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Magnesium binding site 3 out of 4 in the Crystal Structure of the Isocitrate Lyase From the A219C Mutant of Escherichia Coli


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 the Isocitrate Lyase From the A219C Mutant of Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg441

b:21.4
occ:1.00
 O C:HOH1695 2.0 14.9 1.0
O1 C:PYR1446 2.0 16.1 1.0
O C:HOH1696 2.1 14.2 1.0
OD2 C:ASP157 2.1 12.4 1.0
O3 C:PYR1446 2.1 18.8 1.0
O C:HOH1694 2.2 14.6 1.0
C2 C:PYR1446 2.7 15.4 1.0
C1 C:PYR1446 2.7 17.6 1.0
CG C:ASP157 3.2 11.9 1.0
OD1 C:ASP157 3.6 12.9 1.0
O C:HOH1570 3.7 33.7 1.0
O2 C:PYR1446 3.9 12.2 1.0
N C:GLY92 4.1 14.6 1.0
OD2 C:ASP108 4.1 23.9 1.0
C3 C:PYR1446 4.1 18.9 1.0
N C:TRP93 4.2 14.1 1.0
NH1 C:ARG232 4.2 18.1 1.0
OD1 C:ASP108 4.2 16.0 1.0
CA C:GLY92 4.2 13.5 1.0
CB C:ASP157 4.5 9.3 1.0
OE2 C:GLU159 4.5 20.0 1.0
CE1 C:HIS184 4.5 12.2 1.0
CG C:ASP108 4.6 22.7 1.0
C C:GLY92 4.6 14.0 1.0
OE2 C:GLU186 4.6 21.6 1.0
O C:HOH1588 4.7 37.1 1.0
OH C:TYR89 4.9 16.0 1.0
CG C:GLU159 4.9 24.2 1.0

Magnesium binding site 4 out of 4 in 1igw

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Magnesium binding site 4 out of 4 in the Crystal Structure of the Isocitrate Lyase From the A219C Mutant of Escherichia Coli


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 the Isocitrate Lyase From the A219C Mutant of Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg441

b:27.9
occ:1.00
 O1 D:PYR1447 2.0 28.2 1.0
O D:HOH1586 2.1 25.6 1.0
OD2 D:ASP157 2.1 16.0 1.0
O D:HOH1585 2.2 23.1 1.0
O3 D:PYR1447 2.2 26.9 1.0
O D:HOH1584 2.2 22.1 1.0
C1 D:PYR1447 2.7 26.2 1.0
C2 D:PYR1447 2.7 28.1 1.0
CG D:ASP157 3.2 20.6 1.0
OD1 D:ASP157 3.8 23.2 1.0
O2 D:PYR1447 3.9 25.7 1.0
C3 D:PYR1447 3.9 26.2 1.0
N D:GLY92 3.9 22.4 1.0
N D:TRP93 4.0 20.0 1.0
OD2 D:ASP108 4.0 24.2 1.0
CA D:GLY92 4.1 21.0 1.0
O D:HOH1514 4.1 34.1 1.0
OD1 D:ASP108 4.3 29.8 1.0
NH1 D:ARG232 4.3 27.2 1.0
OE2 D:GLU159 4.4 34.8 1.0
C D:GLY92 4.4 19.6 1.0
CB D:ASP157 4.5 20.4 1.0
CE1 D:HIS184 4.5 22.8 1.0
CG D:ASP108 4.5 21.6 1.0
O D:HOH1522 4.6 36.3 1.0
CG D:GLU159 4.6 29.2 1.0
OE2 D:GLU186 4.8 32.1 1.0
CD D:GLU159 4.8 28.4 1.0
CB D:TRP93 4.9 19.5 1.0
CA D:TRP93 4.9 19.3 1.0
OH D:TYR89 4.9 31.0 1.0

Reference:

K.L.Britton, I.S.Abeysinghe, P.J.Baker, V.Barynin, P.Diehl, S.J.Langridge, B.A.Mcfadden, S.E.Sedelnikova, T.J.Stillman, K.Weeradechapon, D.W.Rice. The Structure and Domain Organization of Escherichia Coli Isocitrate Lyase. Acta Crystallogr.,Sect.D V. 57 1209 2001.
ISSN: ISSN 0907-4449
PubMed: 11526312
DOI: 10.1107/S0907444901008642
Page generated: Tue Aug 13 04:58:19 2024

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