Chlorine in PDB 4loc: Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin

Enzymatic activity of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin

All present enzymatic activity of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin:
6.4.1.1;

Protein crystallography data

The structure of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin, PDB code: 4loc was solved by A.D.Lietzan, M.St. Maurice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	43.75 / 2.26
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	83.870, 157.123, 244.714, 90.00, 90.00, 90.00
*R / R_free (%)*	17.6 / 21.6

Other elements in 4loc:

The structure of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin also contains other interesting chemical elements:

Magnesium	(Mg)	4 atoms
Zinc	(Zn)	4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin (pdb code 4loc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin, PDB code: 4loc:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 4loc

Go back to

Chlorine Binding Sites List in 4loc

Chlorine binding site 1 out of 3 in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin

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 Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1103 b:45.9 occ:1.00	O	A:HOH1354	3.2	56.7	1.0
	N	A:LYS989	3.4	37.7	1.0
	N	A:VAL990	3.4	36.1	1.0
	CA	A:TYR987	3.5	34.2	1.0
	C	A:TYR987	3.5	32.6	1.0
	N	A:PRO988	3.6	32.7	1.0
	CB	A:LYS989	3.7	42.3	1.0
	CG2	A:VAL990	3.8	35.1	1.0
	CD1	A:TYR987	3.8	29.0	1.0
	CD	A:PRO988	3.8	34.6	1.0
	CB	A:VAL990	3.9	35.9	1.0
	CB	A:TYR987	3.9	31.9	1.0
	CA	A:LYS989	4.0	38.8	1.0
	O	A:TYR987	4.0	34.5	1.0
	C	A:LYS989	4.2	37.2	1.0
	CA	A:VAL990	4.3	34.4	1.0
	CG	A:TYR987	4.3	29.9	1.0
	C	A:PRO988	4.3	36.2	1.0
	CA	A:PRO988	4.5	34.7	1.0
	CG	A:PRO988	4.5	34.8	1.0
	CE1	A:TYR987	4.8	27.8	1.0
	N	A:TYR987	4.9	32.4	1.0

Chlorine binding site 2 out of 3 in 4loc

Go back to

Chlorine Binding Sites List in 4loc

Chlorine binding site 2 out of 3 in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
C:Cl1104 b:58.9 occ:1.00	N	C:LYS989	3.3	68.1	1.0
	CA	C:TYR987	3.4	63.4	1.0
	C	C:TYR987	3.4	63.8	1.0
	N	C:VAL990	3.4	65.4	1.0
	N	C:PRO988	3.5	64.3	1.0
	CD	C:PRO988	3.6	65.5	1.0
	CB	C:LYS989	3.7	71.1	1.0
	CB	C:TYR987	3.7	62.7	1.0
	CG2	C:VAL990	3.8	60.9	1.0
	CD1	C:TYR987	3.9	60.6	1.0
	CA	C:LYS989	3.9	70.0	1.0
	O	C:TYR987	4.0	62.6	1.0
	CB	C:VAL990	4.1	61.3	1.0
	C	C:LYS989	4.2	68.1	1.0
	C	C:PRO988	4.2	68.3	1.0
	CG	C:TYR987	4.3	61.1	1.0
	CA	C:PRO988	4.4	67.6	1.0
	CA	C:VAL990	4.4	63.3	1.0
	CG	C:PRO988	4.6	68.7	1.0
	N	C:TYR987	4.8	62.9	1.0
	CB	C:PRO988	4.8	69.6	1.0
	CE1	C:TYR987	5.0	58.5	1.0

Chlorine binding site 3 out of 3 in 4loc

Go back to

Chlorine Binding Sites List in 4loc

Chlorine binding site 3 out of 3 in the Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of the Carboxyl Transferase Domain From Rhizobium Etli Pyruvate Carboxylase with Oxamate and Biotin within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
D:Cl1103 b:49.9 occ:1.00	N	D:LYS989	3.2	55.4	1.0
	N	D:VAL990	3.2	47.9	1.0
	C	D:TYR987	3.4	44.4	1.0
	CA	D:TYR987	3.4	43.1	1.0
	N	D:PRO988	3.5	45.7	1.0
	CB	D:TYR987	3.7	41.6	1.0
	CD	D:PRO988	3.7	47.0	1.0
	CG2	D:VAL990	3.7	45.5	1.0
	CB	D:LYS989	3.7	59.3	1.0
	CA	D:LYS989	3.8	56.6	1.0
	CD1	D:TYR987	3.8	41.0	1.0
	CB	D:VAL990	3.9	46.1	1.0
	O	D:TYR987	3.9	46.6	1.0
	C	D:LYS989	4.0	51.5	1.0
	C	D:PRO988	4.1	51.8	1.0
	CA	D:VAL990	4.2	46.9	1.0
	CG	D:TYR987	4.2	41.5	1.0
	CA	D:PRO988	4.4	48.9	1.0
	CG	D:PRO988	4.8	49.4	1.0
	N	D:TYR987	4.8	43.0	1.0
	CB	D:PRO988	4.9	49.7	1.0
	CG	D:LYS989	4.9	63.5	1.0

Reference:

A.D.Lietzan, Y.Lin, M.St. Maurice. The Role of Biotin and Oxamate in the Carboxyltransferase Reaction of Pyruvate Carboxylase. Arch.Biochem.Biophys. V.562C 70 2014.
ISSN: ISSN 0003-9861
PubMed: 25157442
DOI: 10.1016/J.ABB.2014.08.008

Page generated: Sun Jul 21 19:04:52 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