Manganese in PDB 1zjo: Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose-Grease

Enzymatic activity of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose-Grease

All present enzymatic activity of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose-Grease:
2.4.1.40;

Protein crystallography data

The structure of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose-Grease, PDB code: 1zjo was solved by J.A.Letts, N.L.Rose, Y.R.Fang, C.H.Barry, S.N.Borisova, N.O.Seto, M.M.Palcic, S.V.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.00 / 1.64
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	52.570, 149.570, 79.390, 90.00, 90.00, 90.00
*R / R_free (%)*	20.6 / 22.6

Other elements in 1zjo:

The structure of Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose-Grease also contains other interesting chemical elements:

Mercury	(Hg)	5 atoms
Chlorine	(Cl)	2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose-Grease (pdb code 1zjo). 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 Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose-Grease, PDB code: 1zjo:

Manganese binding site 1 out of 1 in 1zjo

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Manganese Binding Sites List in 1zjo

Manganese binding site 1 out of 1 in the Crystal Structure of Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose-Grease

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 Human N-Acetylgalactosaminyltransferase (Gta) Complexed with Galactose-Grease within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn450 b:33.5 occ:0.20	O1A	A:UDP2	2.3	64.8	1.0
	O3B	A:UDP2	2.4	67.7	1.0
	OD1	A:ASP213	2.6	24.0	1.0
	OD1	A:ASP211	2.8	27.5	1.0
	O1B	A:UDP2	2.9	67.3	1.0
	O3'	A:UDP2	2.9	58.7	1.0
	PB	A:UDP2	3.0	67.8	1.0
	OD2	A:ASP213	3.1	27.0	1.0
	CG	A:ASP211	3.2	23.1	1.0
	CG	A:ASP213	3.2	24.2	1.0
	CB	A:ASP211	3.4	21.3	1.0
	C5'	A:UDP2	3.4	60.1	1.0
	PA	A:UDP2	3.5	64.4	1.0
	O3A	A:UDP2	3.7	66.0	1.0
	C3'	A:UDP2	3.8	57.7	1.0
	O5'	A:UDP2	3.9	62.6	1.0
	C4'	A:UDP2	4.0	58.6	1.0
	OD2	A:ASP211	4.1	24.4	1.0
	O2B	A:UDP2	4.6	67.2	1.0
	CB	A:ASP213	4.7	21.9	1.0
	CA	A:ASP211	4.8	19.0	1.0
	O2A	A:UDP2	4.8	65.0	1.0
	O	A:HOH692	4.9	46.7	1.0

Reference:

J.A.Letts, N.L.Rose, Y.R.Fang, C.H.Barry, S.N.Borisova, N.O.Seto, M.M.Palcic, S.V.Evans. Differential Recognition of the Type I and II H Antigen Acceptors By the Human Abo(H) Blood Group A and B Glycosyltransferases. J.Biol.Chem. V. 281 3625 2006.
ISSN: ISSN 0021-9258
PubMed: 16326711
DOI: 10.1074/JBC.M507620200

Page generated: Sat Oct 5 13:17:39 2024

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