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Magnesium in PDB 1xin: Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites

Enzymatic activity of Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites

All present enzymatic activity of Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites:
5.3.1.5;

Protein crystallography data

The structure of Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites, PDB code: 1xin was solved by J.Janin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.40
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 143.450, 143.450, 231.500, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites (pdb code 1xin). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites, PDB code: 1xin:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1xin

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Magnesium binding site 1 out of 4 in the Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg395

b:25.8
occ:1.00
 OD2 A:ASP292 1.9 15.3 1.0
OD2 A:ASP245 2.0 15.2 1.0
OE1 A:GLU217 2.1 16.4 1.0
OE2 A:GLU181 2.2 16.9 1.0
O2 A:XYL397 2.3 32.3 1.0
O4 A:XYL397 2.4 31.5 1.0
CG A:ASP292 3.0 14.2 1.0
CD A:GLU181 3.1 16.2 1.0
OE1 A:GLU181 3.2 17.5 1.0
CG A:ASP245 3.2 13.6 1.0
CD A:GLU217 3.3 16.4 1.0
C2 A:XYL397 3.5 32.8 1.0
C4 A:XYL397 3.5 31.9 1.0
C3 A:XYL397 3.7 32.2 1.0
CB A:ASP292 3.8 12.8 1.0
CB A:ASP245 3.8 10.4 1.0
O3 A:XYL397 3.8 31.6 1.0
O A:HOH454 3.9 15.7 1.0
OE2 A:GLU217 4.0 20.4 1.0
OD1 A:ASP292 4.0 14.9 1.0
O A:HOH586 4.0 37.2 1.0
CG A:GLU217 4.1 14.8 1.0
OD1 A:ASP245 4.1 14.3 1.0
CB A:GLU217 4.3 12.0 1.0
CG A:GLU181 4.4 13.4 1.0
C1 A:XYL397 4.7 32.8 1.0
ND2 A:ASN215 4.7 5.3 1.0
C5 A:XYL397 4.8 29.4 1.0
O A:HOH536 4.8 32.2 1.0

Magnesium binding site 2 out of 4 in 1xin

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Magnesium binding site 2 out of 4 in the Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg395

b:26.2
occ:1.00
 OD2 B:ASP245 1.9 16.4 1.0
OE1 B:GLU217 2.0 16.6 1.0
OD2 B:ASP292 2.1 14.4 1.0
OE2 B:GLU181 2.2 19.4 1.0
O4 B:XYL397 2.4 34.6 1.0
O2 B:XYL397 2.4 38.1 1.0
CD B:GLU181 3.0 18.3 1.0
CG B:ASP245 3.1 13.8 1.0
OE1 B:GLU181 3.2 19.1 1.0
CG B:ASP292 3.2 13.3 1.0
CD B:GLU217 3.2 15.7 1.0
C4 B:XYL397 3.4 35.2 1.0
C2 B:XYL397 3.6 36.0 1.0
O3 B:XYL397 3.7 35.0 1.0
C3 B:XYL397 3.8 35.5 1.0
O B:HOH461 3.8 23.7 1.0
O B:HOH604 3.8 37.2 1.0
CB B:ASP292 3.8 12.0 1.0
CB B:ASP245 3.9 12.5 1.0
OE2 B:GLU217 3.9 22.3 1.0
OD1 B:ASP245 4.1 12.0 1.0
CG B:GLU217 4.1 14.5 1.0
OD1 B:ASP292 4.2 14.0 1.0
CB B:GLU217 4.2 12.0 1.0
CG B:GLU181 4.4 17.1 1.0
C5 B:XYL397 4.7 33.1 1.0
ND2 B:ASN215 4.7 11.9 1.0
C1 B:XYL397 4.7 35.5 1.0
O B:HOH541 4.8 32.2 1.0
O1 B:XYL397 5.0 33.5 1.0

Magnesium binding site 3 out of 4 in 1xin

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Magnesium binding site 3 out of 4 in the Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg395

b:19.6
occ:1.00
 OD2 C:ASP245 2.0 15.8 1.0
OE1 C:GLU217 2.0 18.1 1.0
OD2 C:ASP292 2.1 13.7 1.0
OE2 C:GLU181 2.2 17.9 1.0
O2 C:XYL397 2.3 33.8 1.0
O4 C:XYL397 2.5 26.6 1.0
CD C:GLU181 3.1 16.3 1.0
CD C:GLU217 3.1 17.6 1.0
CG C:ASP292 3.2 13.2 1.0
CG C:ASP245 3.2 13.2 1.0
OE1 C:GLU181 3.3 17.8 1.0
C2 C:XYL397 3.6 32.1 1.0
C4 C:XYL397 3.6 27.5 1.0
CB C:ASP245 3.8 11.3 1.0
CB C:ASP292 3.8 12.2 1.0
OE2 C:GLU217 3.9 22.2 1.0
C3 C:XYL397 3.9 29.5 1.0
O3 C:XYL397 4.0 29.0 1.0
CG C:GLU217 4.1 14.9 1.0
OD1 C:ASP245 4.1 12.8 1.0
O C:HOH469 4.1 19.9 1.0
OD1 C:ASP292 4.2 14.2 1.0
CB C:GLU217 4.2 11.2 1.0
CG C:GLU181 4.4 14.5 1.0
ND2 C:ASN215 4.6 4.9 1.0
C1 C:XYL397 4.6 32.9 1.0
O C:HOH609 4.7 44.2 1.0
O C:HOH552 4.9 27.1 1.0
C5 C:XYL397 4.9 25.2 1.0
O1 C:XYL397 5.0 32.5 1.0

Magnesium binding site 4 out of 4 in 1xin

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Magnesium binding site 4 out of 4 in the Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site- Directed Mutagenesis of Metal Binding Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg395

b:23.8
occ:1.00
 OD2 D:ASP292 1.9 13.0 1.0
OD2 D:ASP245 2.0 14.6 1.0
OE1 D:GLU217 2.0 16.5 1.0
OE2 D:GLU181 2.1 19.4 1.0
O4 D:XYL397 2.3 34.5 1.0
O2 D:XYL397 2.4 35.5 1.0
CD D:GLU181 3.1 16.3 1.0
CG D:ASP292 3.1 11.0 1.0
CD D:GLU217 3.1 15.6 1.0
CG D:ASP245 3.1 15.0 1.0
OE1 D:GLU181 3.4 17.4 1.0
C4 D:XYL397 3.5 34.6 1.0
C2 D:XYL397 3.6 36.1 1.0
O3 D:XYL397 3.6 36.5 1.0
C3 D:XYL397 3.7 35.6 1.0
CB D:ASP245 3.8 13.1 1.0
CB D:ASP292 3.8 10.8 1.0
OE2 D:GLU217 3.8 19.9 1.0
O D:HOH475 4.0 22.2 1.0
CG D:GLU217 4.0 14.7 1.0
OD1 D:ASP292 4.1 10.5 1.0
OD1 D:ASP245 4.2 13.3 1.0
CB D:GLU217 4.2 13.1 1.0
CG D:GLU181 4.4 14.4 1.0
O D:HOH617 4.5 49.4 1.0
C1 D:XYL397 4.7 35.7 1.0
O D:HOH556 4.7 76.3 1.0
ND2 D:ASN215 4.7 7.6 1.0
C5 D:XYL397 4.7 32.6 1.0
O1 D:XYL397 5.0 34.6 1.0

Reference:

J.Jenkins, J.Janin, F.Rey, M.Chiadmi, H.Van Tilbeurgh, I.Lasters, M.De Maeyer, D.Van Belle, S.J.Wodak, M.Lauwereys, P.Stanssens, G.Matthyssens, A.M.Lambeir. Protein Engineering of Xylose (Glucose) Isomerase From Actinoplanes Missouriensis. 1. Crystallography and Site-Directed Mutagenesis of Metal Binding Sites. Biochemistry V. 31 5449 1992.
ISSN: ISSN 0006-2960
PubMed: 1610791
DOI: 10.1021/BI00139A005
Page generated: Sun Aug 10 07:05:47 2025

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