Sodium in PDB 7w45: Complex Structure of A Leaf-Branch Compost Cutinase Variant Lcc ICCG_KIP

Enzymatic activity of Complex Structure of A Leaf-Branch Compost Cutinase Variant Lcc ICCG_KIP

All present enzymatic activity of Complex Structure of A Leaf-Branch Compost Cutinase Variant Lcc ICCG_KIP:
3.1.1.101; 3.1.1.74;

Protein crystallography data

The structure of Complex Structure of A Leaf-Branch Compost Cutinase Variant Lcc ICCG_KIP, PDB code: 7w45 was solved by D.Niu, W.Zeng, J.W.Huang, C.C.Chen, W.D.Liu, R.T.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	35.44 / 1.94
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	40.37, 84.77, 147.512, 90, 90, 90
*R / R_free (%)*	15.4 / 20

Other elements in 7w45:

The structure of Complex Structure of A Leaf-Branch Compost Cutinase Variant Lcc ICCG_KIP also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Complex Structure of A Leaf-Branch Compost Cutinase Variant Lcc ICCG_KIP (pdb code 7w45). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Complex Structure of A Leaf-Branch Compost Cutinase Variant Lcc ICCG_KIP, PDB code: 7w45:

Sodium binding site 1 out of 1 in 7w45

Go back to

Sodium Binding Sites List in 7w45

Sodium binding site 1 out of 1 in the Complex Structure of A Leaf-Branch Compost Cutinase Variant Lcc ICCG_KIP

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Complex Structure of A Leaf-Branch Compost Cutinase Variant Lcc ICCG_KIP within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Na301 b:4.3 occ:1.00	OG	A:SER136	3.0	10.2	1.0
	ND2	A:ASN178	3.2	10.8	1.0
	O	B:HOH463	3.2	13.7	1.0
	O	A:HOH462	3.2	11.4	1.0
	CG	B:LEU84	3.6	12.8	1.0
	CB	A:SER136	3.6	10.0	1.0
	CD1	A:ILE174	3.7	9.1	1.0
	CB	A:ASN178	3.8	10.8	1.0
	CD1	B:LEU84	3.8	13.0	1.0
	CD2	B:LEU84	3.8	14.0	1.0
	CG1	A:ILE174	3.9	9.8	1.0
	CA	A:SER136	3.9	9.7	1.0
	CG	A:ASN178	3.9	10.9	1.0
	CD1	A:LEU139	4.5	12.0	1.0
	O	A:SER136	4.7	9.4	1.0
	OG1	B:THR82	4.7	11.3	1.0
	O	A:HOH424	4.8	25.4	1.0
	C	A:SER136	4.8	9.6	1.0
	CB	B:LEU84	5.0	12.8	1.0

Reference:

W.Zeng, X.Li, Y.Yang, J.Min, J.-W.Huang, W.Liu, D.Niu, X.Yang, X.Han, L.Zhang, L.Dai, C.-C.Chen, R.-T.Guo. Substrate-Binding Mode of A Thermophilic Pet Hydrolase and Engineering the Enzyme to Enhance the Hydrolytic Efficacy. Acs Catalysis V. 12 3033 2022.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.1C05800

Page generated: Wed Oct 9 09:25:54 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy