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Magnesium in PDB 1gll: Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion

Enzymatic activity of Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion

All present enzymatic activity of Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion:
2.7.1.30;

Protein crystallography data

The structure of Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion, PDB code: 1gll was solved by C.E.Bystrom, D.W.Pettigrew, B.P.Branchaud, S.J.Remington, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 99.766, 201.148, 114.340, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion (pdb code 1gll). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion, PDB code: 1gll:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1gll

Go back to Magnesium Binding Sites List in 1gll
Magnesium binding site 1 out of 2 in the Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion within 5.0Å range:
probe atom residue distance (Å) B Occ
Y:Mg602

b:40.6
occ:1.00
O2B Y:ACP601 2.4 47.9 1.0
O3G Y:ACP601 2.6 47.9 1.0
PB Y:ACP601 3.3 47.9 1.0
O1B Y:ACP601 3.4 47.9 1.0
C3B Y:ACP601 3.7 47.9 1.0
PG Y:ACP601 3.8 47.9 1.0
OD2 Y:ASP245 3.8 55.9 1.0
OD1 Y:ASP10 3.9 70.7 1.0
OD2 Y:ASP10 4.0 75.6 1.0
CB Y:ASP245 4.3 41.4 1.0
CG Y:ASP10 4.4 67.2 1.0
CA Y:GLY12 4.5 34.3 1.0
O1G Y:ACP601 4.6 47.9 1.0
CG Y:ASP245 4.6 51.6 1.0
O3A Y:ACP601 4.8 47.9 1.0

Magnesium binding site 2 out of 2 in 1gll

Go back to Magnesium Binding Sites List in 1gll
Magnesium binding site 2 out of 2 in the Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Mg602

b:65.9
occ:1.00
O1G O:ACP601 3.1 60.6 1.0
O2B O:ACP601 3.3 60.6 1.0
OD2 O:ASP245 3.5 32.2 1.0
O2G O:ACP601 3.7 60.6 1.0
PG O:ACP601 4.0 60.6 1.0
CB O:ASP245 4.1 36.5 1.0
CG O:ASP245 4.3 33.2 1.0
OD1 O:ASP10 4.3 88.4 1.0
OD2 O:ASP10 4.4 91.8 1.0
PB O:ACP601 4.4 60.6 1.0
O1B O:ACP601 4.4 60.6 1.0
CA O:GLY12 4.5 53.4 1.0
CG O:ASP10 4.8 84.6 1.0
O3 O:GOL600 4.8 29.9 1.0

Reference:

C.E.Bystrom, D.W.Pettigrew, B.P.Branchaud, P.O'brien, S.J.Remington. Crystal Structures of Escherichia Coli Glycerol Kinase Variant S58-->W in Complex with Nonhydrolyzable Atp Analogues Reveal A Putative Active Conformation of the Enzyme As A Result of Domain Motion. Biochemistry V. 38 3508 1999.
ISSN: ISSN 0006-2960
PubMed: 10090737
DOI: 10.1021/BI982460Z
Page generated: Mon Dec 14 05:58:03 2020

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