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Manganese in PDB 7bjz: Glucose Isomerase S171W in H32

Enzymatic activity of Glucose Isomerase S171W in H32

All present enzymatic activity of Glucose Isomerase S171W in H32:
5.3.1.5;

Protein crystallography data

The structure of Glucose Isomerase S171W in H32, PDB code: 7bjz was solved by M.Sleutel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.87 / 2.13
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 132.85, 132.85, 234.85, 90, 90, 120
R / Rfree (%) 20.3 / 23.3

Manganese Binding Sites:

The binding sites of Manganese atom in the Glucose Isomerase S171W in H32 (pdb code 7bjz). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Glucose Isomerase S171W in H32, PDB code: 7bjz:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 7bjz

Go back to Manganese Binding Sites List in 7bjz
Manganese binding site 1 out of 4 in the Glucose Isomerase S171W in H32


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Glucose Isomerase S171W in H32 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:71.4
occ:1.00
NE2 A:HIS220 2.5 41.0 1.0
OE1 A:GLU217 2.5 67.6 1.0
O A:HOH510 2.6 68.2 1.0
OD2 A:ASP255 2.6 64.2 1.0
OD1 A:ASP255 2.8 59.4 1.0
OD1 A:ASP257 2.9 54.2 1.0
CG A:ASP255 3.0 59.2 1.0
CD2 A:HIS220 3.3 41.5 1.0
OD2 A:ASP257 3.5 57.5 1.0
CD A:GLU217 3.5 57.1 1.0
CE1 A:HIS220 3.5 46.6 1.0
CG A:ASP257 3.5 49.1 1.0
OE2 A:GLU217 4.0 64.7 1.0
NZ A:LYS183 4.4 44.5 1.0
CE A:LYS183 4.4 39.0 1.0
ND2 A:ASN247 4.5 36.3 1.0
CG A:HIS220 4.5 40.8 1.0
CB A:ASP255 4.5 49.5 1.0
ND1 A:HIS220 4.6 46.6 1.0
CG A:GLU217 4.7 48.7 1.0
OD2 A:ASP287 4.7 74.0 1.0
CZ B:PHE26 4.9 70.2 1.0
MN A:MN402 4.9 81.5 1.0

Manganese binding site 2 out of 4 in 7bjz

Go back to Manganese Binding Sites List in 7bjz
Manganese binding site 2 out of 4 in the Glucose Isomerase S171W in H32


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Glucose Isomerase S171W in H32 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn402

b:81.5
occ:1.00
OE2 A:GLU217 2.1 64.7 1.0
OD2 A:ASP287 2.2 74.0 1.0
OD2 A:ASP245 2.2 52.5 1.0
OE1 A:GLU181 2.3 54.6 1.0
CD A:GLU181 3.0 51.8 1.0
OE2 A:GLU181 3.0 52.1 1.0
CG A:ASP287 3.3 58.9 1.0
CD A:GLU217 3.3 57.1 1.0
CG A:ASP245 3.4 44.5 1.0
O A:HOH510 3.6 68.2 1.0
CB A:ASP287 3.7 54.5 1.0
OE1 A:GLU217 3.9 67.6 1.0
CB A:ASP245 4.0 42.4 1.0
OD1 A:ASP287 4.4 62.7 1.0
CG A:GLU181 4.4 46.0 1.0
OD1 A:ASP245 4.4 51.3 1.0
CE1 A:HIS220 4.4 46.6 1.0
CG A:GLU217 4.5 48.7 1.0
CB A:GLU217 4.6 44.4 1.0
ND2 A:ASN215 4.6 42.1 1.0
NE2 A:HIS220 4.9 41.0 1.0
MN A:MN401 4.9 71.4 1.0

Manganese binding site 3 out of 4 in 7bjz

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Manganese binding site 3 out of 4 in the Glucose Isomerase S171W in H32


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Glucose Isomerase S171W in H32 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn401

b:81.3
occ:1.00
OE1 B:GLU217 2.4 60.1 1.0
NE2 B:HIS220 2.5 43.4 1.0
OD2 B:ASP255 2.7 70.8 1.0
OD1 B:ASP255 2.9 66.8 1.0
OD1 B:ASP257 2.9 59.1 1.0
CG B:ASP255 3.1 66.8 1.0
CD2 B:HIS220 3.3 43.8 1.0
CD B:GLU217 3.4 54.4 1.0
CE1 B:HIS220 3.5 43.8 1.0
OD2 B:ASP257 3.6 60.4 1.0
CG B:ASP257 3.7 48.3 1.0
OE2 B:GLU217 3.9 59.9 1.0
NZ B:LYS183 4.4 47.0 1.0
ND2 B:ASN247 4.5 44.0 1.0
CE B:LYS183 4.5 44.7 1.0
CG B:HIS220 4.5 42.7 1.0
OD2 B:ASP287 4.6 71.3 1.0
ND1 B:HIS220 4.6 44.9 1.0
MN B:MN402 4.6 98.3 1.0
CG B:GLU217 4.6 50.5 1.0
CB B:ASP255 4.6 61.2 1.0
CZ A:PHE26 4.7 58.6 1.0
CG B:ASP287 5.0 55.1 1.0

Manganese binding site 4 out of 4 in 7bjz

Go back to Manganese Binding Sites List in 7bjz
Manganese binding site 4 out of 4 in the Glucose Isomerase S171W in H32


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Glucose Isomerase S171W in H32 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn402

b:98.3
occ:1.00
OE2 B:GLU217 2.0 59.9 1.0
OD2 B:ASP287 2.2 71.3 1.0
OE1 B:GLU181 2.3 69.2 1.0
OD2 B:ASP245 2.4 61.8 1.0
O B:HOH501 2.5 46.4 1.0
CD B:GLU181 3.1 60.7 1.0
CD B:GLU217 3.2 54.4 1.0
OE2 B:GLU181 3.2 52.4 1.0
CG B:ASP287 3.2 55.1 1.0
CG B:ASP245 3.5 57.9 1.0
CB B:ASP287 3.7 52.3 1.0
OE1 B:GLU217 3.8 60.1 1.0
CB B:ASP245 4.0 50.8 1.0
CE1 B:HIS220 4.3 43.8 1.0
OD1 B:ASP287 4.3 53.8 1.0
CG B:GLU217 4.4 50.5 1.0
CG B:GLU181 4.5 52.2 1.0
OD1 B:ASP245 4.6 65.1 1.0
CB B:GLU217 4.6 47.7 1.0
MN B:MN401 4.6 81.3 1.0
NE2 B:HIS220 4.6 43.4 1.0
ND2 B:ASN215 4.8 47.3 1.0

Reference:

A.E.S.Van Driessche, N.Van Gerven, R.R.M.Joosten, A.J.M.Sommerdijk, M.Sleutel. Nonclassical Nucleation of Protein Mesocrystals Via Oriented Attachment Biorxiv 2020.
DOI: 10.1101/2020.08.27.267013
Page generated: Sun Oct 6 08:08:43 2024

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