Magnesium in PDB 7uta: Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction

Enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction

All present enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction:
1.18.6.1;

Other elements in 7uta:

The structure of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Iron	(Fe)	40 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction (pdb code 7uta). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction, PDB code: 7uta:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 7uta

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Magnesium Binding Sites List in 7uta

Magnesium binding site 1 out of 4 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
E:Mg302 b:56.8 occ:1.00	O1B	E:ADP303	2.4	73.8	1.0
	OG	E:SER16	2.9	38.5	1.0
	BE	E:0BE304	3.0	30.0	1.0
	OD1	E:ASP43	3.2	53.5	1.0
	OD2	E:ASP39	3.3	47.9	1.0
	PB	E:ADP303	3.5	73.8	1.0
	O2B	E:ADP303	3.6	73.8	1.0
	CB	E:SER16	3.8	40.5	1.0
	O2A	E:ADP303	3.9	73.8	1.0
	CG	E:ASP43	4.1	50.1	1.0
	CG	E:ASP39	4.2	49.2	1.0
	OD2	E:ASP43	4.2	50.3	1.0
	OD2	E:ASP125	4.2	44.9	1.0
	OG	E:SER44	4.5	47.4	1.0
	O3A	E:ADP303	4.5	73.8	1.0
	O3B	E:ADP303	4.6	73.8	1.0
	CB	E:ASP39	4.7	48.0	1.0
	N	E:SER16	4.8	33.1	1.0
	NZ	E:LYS41	4.8	46.7	1.0
	PA	E:ADP303	4.9	73.8	1.0
	CA	E:SER16	4.9	35.9	1.0
	CE	E:LYS41	5.0	46.0	1.0

Magnesium binding site 2 out of 4 in 7uta

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Magnesium Binding Sites List in 7uta

Magnesium binding site 2 out of 4 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
F:Mg301 b:65.1 occ:1.00	O2B	F:ADP302	2.4	81.9	1.0
	BE	F:0BE303	3.1	30.0	1.0
	PB	F:ADP302	3.4	81.9	1.0
	O3B	F:ADP302	3.5	81.9	1.0
	OG	F:SER16	3.7	48.4	1.0
	CB	F:SER16	4.0	45.5	1.0
	O2A	F:ADP302	4.0	81.9	1.0
	CE	F:LYS15	4.0	44.9	1.0
	N	F:SER16	4.2	39.1	1.0
	CB	F:LYS15	4.3	43.4	1.0
	OD1	F:ASP125	4.3	47.5	1.0
	O1B	F:ADP302	4.4	81.9	1.0
	O3A	F:ADP302	4.6	81.9	1.0
	NZ	F:LYS41	4.7	55.8	1.0
	PA	F:ADP302	4.7	81.9	1.0
	CA	F:SER16	4.7	41.3	1.0
	O	F:VAL126	4.8	46.8	1.0
	O1A	F:ADP302	4.8	81.9	1.0
	OD1	F:ASP43	4.9	61.8	1.0
	NZ	F:LYS15	4.9	42.0	1.0

Magnesium binding site 3 out of 4 in 7uta

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Magnesium Binding Sites List in 7uta

Magnesium binding site 3 out of 4 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
G:Mg302 b:62.0 occ:1.00	OG	G:SER16	2.0	41.1	1.0
	O2B	G:ADP303	2.3	73.8	1.0
	CB	G:SER16	3.1	42.0	1.0
	OD1	G:ASP43	3.3	55.3	1.0
	OD2	G:ASP125	3.4	45.0	1.0
	BE	G:0BE304	3.5	30.0	1.0
	PB	G:ADP303	3.8	73.8	1.0
	OD2	G:ASP39	4.0	50.3	1.0
	CG	G:ASP43	4.0	53.9	1.0
	OD2	G:ASP43	4.0	53.6	1.0
	N	G:SER16	4.1	29.5	1.0
	CA	G:SER16	4.1	33.8	1.0
	CG	G:ASP125	4.3	46.6	1.0
	OG	G:SER44	4.4	45.7	1.0
	O3B	G:ADP303	4.4	73.8	1.0
	OD1	G:ASP125	4.5	45.0	1.0
	O1B	G:ADP303	4.6	73.8	1.0
	O1A	G:ADP303	4.6	73.8	1.0
	O3A	G:ADP303	4.7	73.8	1.0
	NZ	G:LYS15	4.8	45.7	1.0
	O2A	G:ADP303	4.8	73.8	1.0
	CG	G:ASP39	4.8	53.7	1.0
	CB	G:ASP39	4.9	51.0	1.0
	PA	G:ADP303	4.9	73.8	1.0
	CE	H:MET156	5.0	52.4	1.0

Magnesium binding site 4 out of 4 in 7uta

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Magnesium Binding Sites List in 7uta

Magnesium binding site 4 out of 4 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
H:Mg301 b:72.8 occ:1.00	O1B	H:ADP302	2.6	93.5	1.0
	OG	H:SER16	2.7	33.5	1.0
	BE	H:0BE303	3.5	30.0	1.0
	O2B	H:ADP302	3.5	93.5	1.0
	O1A	H:ADP302	3.6	93.5	1.0
	PB	H:ADP302	3.6	93.5	1.0
	CB	H:SER16	3.9	37.4	1.0
	OG	H:SER44	4.1	47.6	1.0
	N	H:SER16	4.5	32.9	1.0
	OD1	H:ASP43	4.6	50.8	1.0
	PA	H:ADP302	4.6	93.5	1.0
	OD1	H:ASP125	4.6	48.9	1.0
	O3A	H:ADP302	4.6	93.5	1.0
	NZ	G:LYS10	4.7	42.0	1.0
	O3B	H:ADP302	4.7	93.5	1.0
	CA	H:SER16	4.9	34.2	1.0

Reference:

H.L.Rutledge, B.D.Cook, H.P.M.Nguyen, M.A.Herzik Jr., F.A.Tezcan. Structures of the Nitrogenase Complex Prepared Under Catalytic Turnover Conditions. Science V. 377 865 2022.
ISSN: ESSN 1095-9203
PubMed: 35901182
DOI: 10.1126/SCIENCE.ABQ7641

Page generated: Thu Oct 3 10:12:32 2024

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