Chlorine in PDB 1fp8: Structure of the Amylomaltase From Thermus Thermophilus HB8 in Space Group P21212

Enzymatic activity of Structure of the Amylomaltase From Thermus Thermophilus HB8 in Space Group P21212

All present enzymatic activity of Structure of the Amylomaltase From Thermus Thermophilus HB8 in Space Group P21212:
2.4.1.25;

Protein crystallography data

The structure of Structure of the Amylomaltase From Thermus Thermophilus HB8 in Space Group P21212, PDB code: 1fp8 was solved by J.C.M.Uitdehaag, G.J.Euverink, B.A.Van Der Veen, M.Van Der Maarel, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 2.30
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	115.234, 93.670, 53.463, 90.00, 90.00, 90.00
*R / R_free (%)*	19.4 / 23.2

Other elements in 1fp8:

The structure of Structure of the Amylomaltase From Thermus Thermophilus HB8 in Space Group P21212 also contains other interesting chemical elements:

Mercury

(Hg)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Amylomaltase From Thermus Thermophilus HB8 in Space Group P21212 (pdb code 1fp8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of the Amylomaltase From Thermus Thermophilus HB8 in Space Group P21212, PDB code: 1fp8:

Chlorine binding site 1 out of 1 in 1fp8

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Chlorine Binding Sites List in 1fp8

Chlorine binding site 1 out of 1 in the Structure of the Amylomaltase From Thermus Thermophilus HB8 in Space Group P21212

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Amylomaltase From Thermus Thermophilus HB8 in Space Group P21212 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl502 b:15.6 occ:1.00	NE2	A:HIS394	2.4	27.0	1.0
	OD2	A:ASP395	2.8	31.4	1.0
	OD1	A:ASP395	3.1	27.0	1.0
	CE1	A:HIS394	3.3	23.7	1.0
	HG	A:HG501	3.3	94.1	1.0
	CG	A:ASP395	3.3	26.4	1.0
	CD2	A:HIS394	3.4	19.8	1.0
	CE1	A:TYR59	3.5	24.9	1.0
	CZ	A:TYR59	3.6	22.6	1.0
	CD1	A:TYR59	3.8	23.1	1.0
	CE2	A:TYR59	4.0	20.3	1.0
	OH	A:TYR59	4.1	21.8	1.0
	CG	A:TYR59	4.2	22.8	1.0
	CD2	A:TYR59	4.3	21.5	1.0
	CH2	A:TRP473	4.3	21.2	1.0
	ND1	A:HIS394	4.4	24.9	1.0
	CG	A:HIS394	4.5	24.9	1.0
	ND2	A:ASN464	4.7	27.0	1.0
	O	A:HOH641	4.8	58.0	1.0
	CB	A:ASP395	4.8	27.6	1.0

Reference:

J.C.M.Uitdehaag, G.J.Euverink, B.A.Van Der Veen, M.Van Der Maarel, B.W.Dijkstra. Structure and Mechanism of the Amylomaltase From Thermus Thermophilus HB8 To Be Published.

Page generated: Sat Dec 12 08:35:25 2020

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