Manganese in PDB 3wak: Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) in the Apo Form

Enzymatic activity of Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) in the Apo Form

All present enzymatic activity of Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) in the Apo Form:
2.4.1.119;

Protein crystallography data

The structure of Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) in the Apo Form, PDB code: 3wak was solved by S.Matsumoto, A.Shimada, D.Kohda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	49.90 / 3.41
*Space group*	P 4₃ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	123.357, 123.357, 182.496, 90.00, 90.00, 90.00
*R / R_free (%)*	21.9 / 27.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) in the Apo Form (pdb code 3wak). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) in the Apo Form, PDB code: 3wak:

Manganese binding site 1 out of 1 in 3wak

Go back to

Manganese Binding Sites List in 3wak

Manganese binding site 1 out of 1 in the Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) in the Apo Form

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Archaeoglobus Fulgidus Oligosaccharyltransferase (O29867_ARCFU) in the Apo Form within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn1200 b:77.4 occ:1.00	OD2	A:ASP47	1.9	0.4	1.0
	OD2	A:ASP161	1.9	93.7	1.0
	NE2	A:HIS163	2.0	76.3	1.0
	CE1	A:HIS163	2.7	73.7	1.0
	CG	A:ASP47	2.9	1.0	1.0
	CG	A:ASP161	3.0	89.3	1.0
	CD2	A:HIS163	3.0	77.6	1.0
	CB	A:ASP47	3.4	92.0	1.0
	OD1	A:ASP161	3.4	93.3	1.0
	ND1	A:HIS163	3.9	66.5	1.0
	OD1	A:ASP47	4.0	0.6	1.0
	CG	A:HIS163	4.0	69.7	1.0
	CE1	A:HIS162	4.1	75.0	1.0
	CB	A:ASP161	4.2	81.2	1.0
	ND1	A:HIS162	4.5	79.8	1.0
	CA	A:ASP47	4.9	85.8	1.0

Reference:

S.Matsumoto, A.Shimada, J.Nyirenda, M.Igura, Y.Kawano, D.Kohda. Crystal Structures of An Archaeal Oligosaccharyltransferase Provide Insights Into the Catalytic Cycle of N-Linked Protein Glycosylation Proc.Natl.Acad.Sci.Usa V. 110 17868 2013.
ISSN: ISSN 0027-8424
PubMed: 24127570
DOI: 10.1073/PNAS.1309777110

Page generated: Sat Oct 5 18:26:26 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1

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