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Arsenic in PDB 1glj: 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: 1glj 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 (°) 99.668, 200.699, 114.733, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1glj:

The structure of Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Arsenic Binding Sites:

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

Arsenic binding site 1 out of 2 in 1glj

Go back to Arsenic Binding Sites List in 1glj
Arsenic 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 Arsenic with other atoms in the As 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:As601

b:50.4
occ:1.00
AS1 Y:ATS601 0.0 50.4 1.0
OG1 Y:ATS601 1.7 50.4 1.0
OG2 Y:ATS601 1.7 50.4 1.0
OG3 Y:ATS601 1.7 50.4 1.0
C3B Y:ATS601 1.9 50.4 1.0
OB1 Y:ATS601 2.7 50.4 1.0
PB Y:ATS601 2.9 50.4 1.0
N Y:THR13 3.6 17.4 1.0
N Y:THR14 3.7 26.7 1.0
OG1 Y:THR14 3.9 40.8 1.0
OG1 Y:THR267 3.9 49.0 1.0
MG Y:MG602 3.9 27.4 1.0
OB2 Y:ATS601 3.9 50.4 1.0
O13 Y:ATS601 3.9 50.4 1.0
OG1 Y:THR13 4.0 18.2 1.0
CA Y:GLY12 4.1 32.7 1.0
C Y:GLY12 4.1 29.5 1.0
CB Y:THR13 4.2 17.7 1.0
CA Y:THR13 4.2 17.3 1.0
CB Y:THR267 4.4 21.9 1.0
C Y:THR13 4.5 28.5 1.0
N Y:SER15 4.6 33.1 1.0
CA Y:THR14 4.7 27.6 1.0
OG Y:SER15 4.7 34.8 1.0
CB Y:THR14 4.7 36.7 1.0
O11 Y:ATS601 4.7 50.4 1.0
CG2 Y:THR14 4.9 33.5 1.0

Arsenic binding site 2 out of 2 in 1glj

Go back to Arsenic Binding Sites List in 1glj
Arsenic 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 Arsenic with other atoms in the As 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:As601

b:64.3
occ:1.00
AS1 O:ATS601 0.0 64.3 1.0
OG1 O:ATS601 1.7 64.3 1.0
OG3 O:ATS601 1.7 64.3 1.0
OG2 O:ATS601 1.8 64.3 1.0
C3B O:ATS601 1.9 64.3 1.0
PB O:ATS601 3.0 64.3 1.0
OB1 O:ATS601 3.0 64.3 1.0
OG1 O:THR14 3.4 61.5 1.0
N O:THR13 3.7 40.0 1.0
OB2 O:ATS601 3.8 64.3 1.0
N O:THR14 3.9 46.4 1.0
CB O:THR13 4.1 39.5 1.0
O11 O:ATS601 4.3 64.3 1.0
CA O:THR13 4.3 39.2 1.0
O13 O:ATS601 4.3 64.3 1.0
OG1 O:THR267 4.4 49.2 1.0
C O:GLY12 4.4 49.1 1.0
CA O:GLY12 4.5 52.4 1.0
CB O:THR14 4.5 57.9 1.0
OG1 O:THR13 4.5 35.9 1.0
C O:THR13 4.6 45.7 1.0
CG2 O:THR14 4.7 52.9 1.0
CA O:THR14 4.7 47.6 1.0
PA O:ATS601 5.0 64.3 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: Tue Oct 27 16:46:40 2020

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