Chlorine in PDB 4f5z: Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (L95V, A172V).

Enzymatic activity of Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (L95V, A172V).

All present enzymatic activity of Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (L95V, A172V).:
3.8.1.5;

Protein crystallography data

The structure of Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (L95V, A172V)., PDB code: 4f5z was solved by D.Kulik, I.Kuta-Smatanova, P.Rezacova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	17.17 / 1.20
*Space group*	P 1
*Cell size a, b, c (Å), α, β, γ (°)*	42.663, 44.489, 46.389, 115.28, 98.61, 109.55
*R / R_free (%)*	12 / 15.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (L95V, A172V). (pdb code 4f5z). 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 Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (L95V, A172V)., PDB code: 4f5z:

Chlorine binding site 1 out of 1 in 4f5z

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Chlorine Binding Sites List in 4f5z

Chlorine binding site 1 out of 1 in the Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (L95V, A172V).

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (L95V, A172V). within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl301 b:9.3 occ:0.40	O2	A:BEZ302	1.0	8.9	0.6
	C	A:BEZ302	1.9	8.5	0.6
	O	A:HOH1140	2.4	45.1	0.4
	O1	A:BEZ302	2.4	8.2	0.6
	O	A:HOH1145	3.1	14.7	0.4
	C1	A:BEZ302	3.2	8.5	0.6
	ND2	A:ASN41	3.2	7.3	1.0
	NE1	A:TRP107	3.4	6.2	1.0
	N	A:PRO206	3.4	7.0	1.0
	CA	A:PRO206	3.6	7.2	1.0
	CD	A:PRO206	3.6	7.0	1.0
	C	A:PHE205	3.7	6.6	1.0
	CB	A:PHE205	3.8	7.0	1.0
	CZ	A:PHE168	3.8	8.4	1.0
	CD1	A:LEU209	3.9	8.5	1.0
	CD1	A:TRP107	3.9	5.6	1.0
	CB	A:PRO206	3.9	7.4	1.0
	C2	A:BEZ302	3.9	9.6	0.6
	CB	A:ASN41	4.0	6.5	1.0
	O	A:PHE205	4.0	7.2	1.0
	CG	A:ASN41	4.1	6.2	1.0
	C6	A:BEZ302	4.1	10.4	0.6
	CG	A:LEU209	4.2	7.1	1.0
	CE2	A:PHE168	4.2	9.3	1.0
	CG	A:PRO206	4.4	7.6	1.0
	CE2	A:PHE149	4.4	9.8	1.0
	CA	A:PHE205	4.4	6.9	1.0
	CD2	A:LEU209	4.5	8.7	1.0
	CE2	A:TRP107	4.6	6.9	1.0
	CE1	A:PHE168	4.7	9.2	1.0
	OD2	A:ASP106	4.8	6.2	1.0
	OD1	A:ASP106	4.8	10.7	1.0
	CG	A:PHE205	4.9	6.7	1.0

Reference:

T.Koudelakova, R.Chaloupkova, J.Brezovsky, Z.Prokop, E.Sebestova, M.Hesseler, M.Khabiri, M.Plevaka, D.Kulik, I.Kuta Smatanova, P.Rezacova, R.Ettrich, U.T.Bornscheuer, J.Damborsky. Engineering Enzyme Stability and Resistance to An Organic Cosolvent By Modification of Residues in the Access Tunnel. Angew.Chem.Int.Ed.Engl. V. 52 1959 2013.
ISSN: ISSN 1433-7851
PubMed: 23303607
DOI: 10.1002/ANIE.201206708

Page generated: Sat Dec 12 10:36:31 2020

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