Magnesium in PDB 8pfg: Autoinhibited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Encounter Complex), Not Fully Complementary Scaffold

Enzymatic activity of Autoinhibited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Encounter Complex), Not Fully Complementary Scaffold

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

Other elements in 8pfg:

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

Zinc

(Zn)

1 atom

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 1 in 8pfg

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Magnesium Binding Sites List in 8pfg

Magnesium binding site 1 out of 1 in the Autoinhibited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Encounter Complex), Not Fully Complementary Scaffold

Mono view

Stereo pair view

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

probe	atom	residue	distance (Å)	B	Occ
J:Mg1502 b:113.8 occ:1.00	OP1	R:U17	2.0	107.9	1.0
	OD1	J:ASP460	2.2	108.4	1.0
	OD1	J:ASP464	2.2	102.2	1.0
	OD2	J:ASP460	2.2	108.1	1.0
	OD2	J:ASP462	2.3	104.3	1.0
	CB	J:ASP462	2.4	96.3	1.0
	CG	J:ASP460	2.4	105.8	1.0
	CG	J:ASP462	2.7	98.2	1.0
	O3'	R:G16	2.7	98.6	1.0
	P	R:U17	2.9	114.2	1.0
	CG	J:ASP464	3.0	94.0	1.0
	OD2	J:ASP464	3.0	93.5	1.0
	O5'	R:U17	3.7	117.4	1.0
	CA	J:ASP462	3.7	90.3	1.0
	CB	J:ASP460	3.8	93.9	1.0
	O	J:ASP460	3.9	103.6	1.0
	C3'	R:G16	3.9	95.4	1.0
	OD1	J:ASP462	3.9	96.2	1.0
	C4'	R:G16	4.1	95.7	1.0
	O	J:ASP462	4.1	95.9	1.0
	C	J:ASP462	4.1	91.3	1.0
	OP2	R:U17	4.2	113.4	1.0
	C5'	R:G16	4.3	99.0	1.0
	N	J:ASP462	4.3	99.3	1.0
	C	J:ASP460	4.4	97.5	1.0
	CB	J:ASP464	4.4	83.6	1.0
	CA	J:ASP460	4.5	93.4	1.0
	N	J:ASP460	4.6	98.3	1.0
	N	J:ASP464	4.7	90.6	1.0
	O2'	R:G16	4.7	105.0	1.0
	C2'	R:G16	5.0	100.5	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 Aug 15 12:23:56 2025

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