Magnesium in PDB 1lv5: Crystal Structure of the Closed Conformation of Bacillus Dna Polymerase I Fragment Bound to Dna and Dctp

Enzymatic activity of Crystal Structure of the Closed Conformation of Bacillus Dna Polymerase I Fragment Bound to Dna and Dctp

All present enzymatic activity of Crystal Structure of the Closed Conformation of Bacillus Dna Polymerase I Fragment Bound to Dna and Dctp:
2.7.7.7;

Protein crystallography data

The structure of Crystal Structure of the Closed Conformation of Bacillus Dna Polymerase I Fragment Bound to Dna and Dctp, PDB code: 1lv5 was solved by S.J.Johnson, J.S.Taylor, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	39.70 / 1.95
*Space group*	P 3₁
*Cell size a, b, c (Å), α, β, γ (°)*	91.681, 91.681, 190.116, 90.00, 90.00, 120.00
*R / R_free (%)*	21.8 / 26.1

Other elements in 1lv5:

The structure of Crystal Structure of the Closed Conformation of Bacillus Dna Polymerase I Fragment Bound to Dna and Dctp also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Closed Conformation of Bacillus Dna Polymerase I Fragment Bound to Dna and Dctp (pdb code 1lv5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Closed Conformation of Bacillus Dna Polymerase I Fragment Bound to Dna and Dctp, PDB code: 1lv5:

Magnesium binding site 1 out of 1 in 1lv5

Go back to

Magnesium Binding Sites List in 1lv5

Magnesium binding site 1 out of 1 in the Crystal Structure of the Closed Conformation of Bacillus Dna Polymerase I Fragment Bound to Dna and Dctp

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 Closed Conformation of Bacillus Dna Polymerase I Fragment Bound to Dna and Dctp within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg205 b:34.5 occ:1.00	OD1	A:ASP830	2.7	22.2	1.0
	O2A	A:DCP201	2.7	30.1	1.0
	OD2	A:ASP653	2.9	36.3	1.0
	MN	A:MN1	3.5	40.6	1.0
	C3'	C:DA29	3.6	32.5	1.0
	PA	A:DCP201	3.6	28.8	1.0
	CG	A:ASP830	3.9	23.2	1.0
	O1A	A:DCP201	3.9	29.0	1.0
	CG	A:ASP653	3.9	36.1	1.0
	C4'	C:DA29	4.1	32.9	1.0
	O5'	A:DCP201	4.1	29.3	1.0
	C5'	C:DA29	4.1	30.9	1.0
	CB	A:GLU831	4.3	32.1	1.0
	O	A:VAL828	4.4	28.4	1.0
	OD1	A:ASP653	4.4	36.4	1.0
	OD2	A:ASP830	4.4	23.9	1.0
	C5'	A:DCP201	4.5	27.1	1.0
	OP1	C:DA29	4.6	32.4	1.0
	O	A:ASP830	4.7	25.2	1.0
	C	A:ASP830	4.8	26.4	1.0
	O5'	C:DA29	4.8	31.5	1.0
	O2G	A:DCP201	4.8	33.2	1.0
	C2'	C:DA29	4.8	34.3	1.0
	O2B	A:DCP201	4.9	33.0	1.0

Reference:

S.J.Johnson, J.S.Taylor, L.S.Beese. Processive Dna Synthesis Observed in A Polymerase Crystal Suggests A Mechanism For the Prevention of Frameshift Mutations Proc.Natl.Acad.Sci.Usa V. 100 3895 2003.
ISSN: ISSN 0027-8424
PubMed: 12649320
DOI: 10.1073/PNAS.0630532100

Page generated: Tue Aug 13 08:35:10 2024

Last articles

Cl in 3MSK
Cl in 3MN1
Cl in 3MS7
Cl in 3MR1
Cl in 3MQE
Cl in 3MPJ
Cl in 3MQZ
Cl in 3MQD
Cl in 3MPQ
Cl in 3MPN

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy