Chlorine in PDB 2idx: Structure of Human Atp:Cobalamin Adenosyltransferase Bound to Atp.

Enzymatic activity of Structure of Human Atp:Cobalamin Adenosyltransferase Bound to Atp.

All present enzymatic activity of Structure of Human Atp:Cobalamin Adenosyltransferase Bound to Atp.:
2.5.1.17;

Protein crystallography data

The structure of Structure of Human Atp:Cobalamin Adenosyltransferase Bound to Atp., PDB code: 2idx was solved by H.L.Schubert, C.P.Hill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	30.00 / 2.50
*Space group*	P 3₁ 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	111.238, 111.238, 115.526, 90.00, 90.00, 120.00
*R / R_free (%)*	19.7 / 25.1

Other elements in 2idx:

The structure of Structure of Human Atp:Cobalamin Adenosyltransferase Bound to Atp. also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Human Atp:Cobalamin Adenosyltransferase Bound to Atp. (pdb code 2idx). 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 Human Atp:Cobalamin Adenosyltransferase Bound to Atp., PDB code: 2idx:

Chlorine binding site 1 out of 1 in 2idx

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Chlorine Binding Sites List in 2idx

Chlorine binding site 1 out of 1 in the Structure of Human Atp:Cobalamin Adenosyltransferase Bound to Atp.

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Human Atp:Cobalamin Adenosyltransferase Bound to Atp. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl601 b:33.4 occ:1.00	NH2	B:ARG195	3.2	22.1	1.0
	NH2	A:ARG195	3.2	30.0	1.0
	NH2	C:ARG195	3.2	19.8	1.0
	O	A:HOH619	3.2	24.5	1.0
	O	C:HOH674	3.3	29.2	1.0
	O	B:HOH674	3.3	29.0	1.0
	NE	A:ARG191	4.0	29.7	1.0
	NE	B:ARG191	4.0	21.4	1.0
	CD	B:ARG191	4.1	21.9	1.0
	OE1	B:GLU84	4.2	25.7	1.0
	CD	A:ARG191	4.2	25.2	1.0
	NE	C:ARG191	4.2	23.4	1.0
	CZ	B:ARG195	4.3	24.0	1.0
	CZ	C:ARG195	4.4	20.5	1.0
	CZ	A:ARG195	4.4	28.3	1.0
	OE1	C:GLU84	4.5	32.3	1.0
	NE	B:ARG195	4.5	24.5	1.0
	CD	C:ARG191	4.5	20.0	1.0
	OE1	A:GLU84	4.5	30.9	1.0
	CZ	A:ARG191	4.8	28.4	1.0
	NE	C:ARG195	4.8	20.1	1.0
	CZ	B:ARG191	4.8	17.8	1.0
	NE	A:ARG195	4.8	27.3	1.0
	CG	B:ARG191	4.9	19.8	1.0
	CZ	C:ARG191	4.9	21.7	1.0
	CG	A:ARG191	4.9	24.1	1.0

Reference:

H.L.Schubert, C.P.Hill. Structure of Atp-Bound Human Atp:Cobalamin Adenosyltransferase. Biochemistry V. 45 15188 2006.
ISSN: ISSN 0006-2960
PubMed: 17176040
DOI: 10.1021/BI061396F

Page generated: Sat Dec 12 09:08:33 2020

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