Chlorine in PDB 4pip: Engineered Egtd Variant Egtd-M252V,E282A in Complex with Tryptophan and Sah

Enzymatic activity of Engineered Egtd Variant Egtd-M252V,E282A in Complex with Tryptophan and Sah

All present enzymatic activity of Engineered Egtd Variant Egtd-M252V,E282A in Complex with Tryptophan and Sah:
2.1.1.44;

Protein crystallography data

The structure of Engineered Egtd Variant Egtd-M252V,E282A in Complex with Tryptophan and Sah, PDB code: 4pip was solved by A.Vit, F.P.Seebeck, W.Blankenfeldt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	41.86 / 1.80
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	79.045, 67.634, 112.125, 90.00, 109.24, 90.00
*R / R_free (%)*	19.4 / 23.9

Other elements in 4pip:

The structure of Engineered Egtd Variant Egtd-M252V,E282A in Complex with Tryptophan and Sah also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Engineered Egtd Variant Egtd-M252V,E282A in Complex with Tryptophan and Sah (pdb code 4pip). 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 Engineered Egtd Variant Egtd-M252V,E282A in Complex with Tryptophan and Sah, PDB code: 4pip:

Chlorine binding site 1 out of 1 in 4pip

Go back to

Chlorine Binding Sites List in 4pip

Chlorine binding site 1 out of 1 in the Engineered Egtd Variant Egtd-M252V,E282A in Complex with Tryptophan and Sah

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Engineered Egtd Variant Egtd-M252V,E282A in Complex with Tryptophan and Sah within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
C:Cl401 b:22.6 occ:1.00	H	C:HIS0	1.5	46.1	1.0
	ND1	C:HIS0	2.2	35.1	1.0
	N	C:GLY-1	2.2	36.1	1.0
	N	C:HIS0	2.3	38.5	1.0
	O	C:HOH592	2.5	20.2	1.0
	CA	C:GLY-1	3.0	37.3	1.0
	C	C:GLY-1	3.1	37.5	1.0
	CG	C:HIS0	3.1	36.6	1.0
	H	C:MET1	3.1	42.4	1.0
	CE1	C:HIS0	3.2	34.4	1.0
	HB3	C:HIS0	3.2	45.0	1.0
	CA	C:HIS0	3.3	38.2	1.0
	HA2	C:GLY-1	3.4	44.7	1.0
	HE1	C:HIS0	3.4	41.3	1.0
	CB	C:HIS0	3.4	37.5	1.0
	N	C:MET1	3.8	35.3	1.0
	HA	C:HIS0	4.1	45.8	1.0
	C	C:HIS0	4.1	38.0	1.0
	O	C:HOH630	4.2	36.0	1.0
	O	C:GLY-1	4.3	37.7	1.0
	CD2	C:HIS0	4.3	36.2	1.0
	NE2	C:HIS0	4.3	35.0	1.0
	HB2	C:HIS0	4.3	45.0	1.0
	O	C:HOH565	4.5	26.7	1.0
	O	C:HOH605	4.5	50.1	1.0

Reference:

A.Vit, L.Misson, W.Blankenfeldt, F.P.Seebeck. Ergothioneine Biosynthetic Methyltransferase Egtd Reveals the Structural Basis of Aromatic Amino Acid Betaine Biosynthesis. Chembiochem 2014.
ISSN: ESSN 1439-7633
PubMed: 25404173
DOI: 10.1002/CBIC.201402522

Page generated: Fri Jul 26 00:01:04 2024

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