Magnesium in PDB 6bbl: Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene

Enzymatic activity of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene

All present enzymatic activity of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene:
1.18.6.1;

Protein crystallography data

The structure of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene, PDB code: 6bbl was solved by O.A.Zadvornyy, S.M.Keable, J.Vertemara, B.J.Eilers, D.Karamatullah, A.J.Rasmussen, L.De Gioia, G.Zampella, L.C.Seefeldt, J.W.Peters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	39.76 / 1.68
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	76.781, 128.251, 107.272, 90.00, 109.11, 90.00
*R / R_free (%)*	15.1 / 18.5

Other elements in 6bbl:

The structure of Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Iron	(Fe)	32 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene (pdb code 6bbl). 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 A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene, PDB code: 6bbl:

Magnesium binding site 1 out of 1 in 6bbl

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Magnesium Binding Sites List in 6bbl

Magnesium binding site 1 out of 1 in the Crystal Structure of the A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene

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 A-96GLN Mofe Protein Variant in the Presence of the Substrate Acetylene within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Mg602 b:42.4 occ:1.00	O	B:HOH872	2.2	27.6	1.0
	O	B:HOH1000	3.1	18.9	1.0
	HE3	B:LYS365	3.2	28.0	1.0
	O	D:HOH1295	3.2	27.4	1.0
	HZ3	B:TRP361	3.3	24.2	1.0
	HZ1	B:LYS365	3.4	28.7	1.0
	HD13	B:LEU505	3.5	19.6	1.0
	HG23	B:ILE501	3.5	20.3	1.0
	HD22	B:LEU505	3.6	19.8	1.0
	HB2	B:LEU505	3.6	20.8	1.0
	O	D:HOH1073	3.8	25.1	1.0
	HE3	B:TRP361	3.8	21.2	1.0
	HE2	B:LYS365	3.8	28.0	1.0
	CE	B:LYS365	3.9	23.4	1.0
	O	B:HOH1079	4.0	27.6	1.0
	NZ	B:LYS365	4.0	23.9	1.0
	CZ3	B:TRP361	4.1	20.1	1.0
	HG22	B:ILE501	4.1	20.3	1.0
	CG2	B:ILE501	4.2	16.9	1.0
	O	B:HOH1257	4.2	28.5	1.0
	HG21	B:ILE501	4.2	20.3	1.0
	O	C:HOH1040	4.3	52.2	1.0
	CE3	B:TRP361	4.3	17.7	1.0
	HZ2	B:LYS365	4.3	28.7	1.0
	CD1	B:LEU505	4.4	16.4	1.0
	CD2	B:LEU505	4.5	16.5	1.0
	CB	B:LEU505	4.5	17.4	1.0
	CG	B:LEU505	4.7	16.0	1.0
	HZ3	B:LYS365	4.8	28.7	1.0
	HD12	B:LEU505	4.9	19.6	1.0
	HD11	B:LEU505	5.0	19.6	1.0
	O	B:ILE501	5.0	14.9	1.0
	HD23	B:LEU505	5.0	19.8	1.0

Reference:

S.M.Keable, J.Vertemara, O.A.Zadvornyy, B.J.Eilers, K.Danyal, A.J.Rasmussen, L.De Gioia, G.Zampella, L.C.Seefeldt, J.W.Peters. Structural Characterization of the Nitrogenase Molybdenum-Iron Protein with the Substrate Acetylene Trapped Near the Active Site. J. Inorg. Biochem. V. 180 129 2017.
ISSN: ISSN 1873-3344
PubMed: 29275221
DOI: 10.1016/J.JINORGBIO.2017.12.008

Page generated: Mon Sep 30 19:40:07 2024

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