Magnesium in PDB 8pfj: Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah)

Enzymatic activity of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah)

All present enzymatic activity of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah):
2.7.7.6;

Other elements in 8pfj:

The structure of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah) (pdb code 8pfj). 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 Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah), PDB code: 8pfj:

Magnesium binding site 1 out of 1 in 8pfj

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Magnesium Binding Sites List in 8pfj

Magnesium binding site 1 out of 1 in the Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah)

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
J:Mg1503 b:149.1 occ:1.00	OD1	J:ASP462	2.0	137.8	1.0
	OD2	J:ASP460	2.0	142.9	1.0
	OD1	J:ASP460	2.0	140.1	1.0
	CG	J:ASP460	2.1	140.5	1.0
	OD2	J:ASP462	2.1	140.3	1.0
	CG	J:ASP462	2.3	136.4	1.0
	P	R:U17	2.5	96.1	1.0
	OP1	R:U17	2.5	97.3	1.0
	O3'	R:G16	2.5	98.6	1.0
	OP2	R:U17	2.6	96.7	1.0
	OD1	J:ASP464	3.2	129.2	1.0
	CB	J:ASP460	3.3	135.7	1.0
	O	J:ASP460	3.4	138.3	1.0
	C3'	R:G16	3.7	100.7	1.0
	CB	J:ASP462	3.8	131.8	1.0
	CG	J:ASP464	3.9	128.5	1.0
	C	J:ASP460	3.9	132.7	1.0
	CA	J:ASP460	4.0	131.4	1.0
	O5'	R:U17	4.1	99.2	1.0
	C4'	R:G16	4.1	100.7	1.0
	N	J:ASP460	4.1	131.5	1.0
	OD2	J:ASP464	4.1	130.5	1.0
	C5'	R:G16	4.3	100.6	1.0
	N	J:ASP462	4.4	127.1	1.0
	O2'	R:G16	4.6	101.2	1.0
	CA	J:ASP462	4.6	129.1	1.0
	C2'	R:G16	4.8	102.6	1.0
	O	J:ASP462	4.9	134.5	1.0
	C	J:ASP462	4.9	132.0	1.0
	C5'	R:U17	4.9	98.1	1.0

Reference:

P.K.Zuber, N.Said, T.Hilal, B.Wang, B.Loll, J.Gonzalez-Higueras, C.A.Ramirez-Sarmiento, G.A.Belogurov, I.Artsimovitch, M.C.Wahl, S.H.Knauer. Concerted Transformation of A Hyper-Paused Transcription Complex and Its Reinforcing Protein. Nat Commun V. 15 3040 2024.
ISSN: ESSN 2041-1723
PubMed: 38589445
DOI: 10.1038/S41467-024-47368-4

Page generated: Fri Oct 4 16:03:03 2024

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