Magnesium in PDB 9cv1: Crystal Structure of the Metallo-Beta-Lactamase Vim-15 with L- Captopril

Enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase Vim-15 with L- Captopril

All present enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase Vim-15 with L- Captopril:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Metallo-Beta-Lactamase Vim-15 with L- Captopril, PDB code: 9cv1 was solved by S.B.Silwal, J.C.Nix, R.C.Page, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	39.63 / 1.29
*Space group*	I 2 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	67.75, 77.51, 79.26, 90, 90, 90
*R / R_free (%)*	17.4 / 19.7

Other elements in 9cv1:

The structure of Crystal Structure of the Metallo-Beta-Lactamase Vim-15 with L- Captopril also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Metallo-Beta-Lactamase Vim-15 with L- Captopril (pdb code 9cv1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Metallo-Beta-Lactamase Vim-15 with L- Captopril, PDB code: 9cv1:

Magnesium binding site 1 out of 1 in 9cv1

Go back to

Magnesium Binding Sites List in 9cv1

Magnesium binding site 1 out of 1 in the Crystal Structure of the Metallo-Beta-Lactamase Vim-15 with L- Captopril

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Metallo-Beta-Lactamase Vim-15 with L- Captopril within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg304 b:5.4 occ:1.00	ND1	A:HIS251	2.0	15.1	1.0
	O	A:HOH544	2.2	8.6	1.0
	O	A:HOH545	2.3	9.3	1.0
	CE1	A:HIS251	2.8	14.0	1.0
	CG	A:HIS251	3.1	16.6	1.0
	CB	A:HIS251	3.6	17.6	1.0
	CA	A:HIS251	3.9	14.9	1.0
	NE2	A:HIS251	4.0	16.0	1.0
	CD2	A:HIS251	4.2	14.7	1.0
	O	A:HIS251	4.4	14.9	1.0
	C	A:HIS251	4.6	13.7	1.0
	ND2	A:ASN254	4.9	21.7	1.0
	CD2	A:LEU203	4.9	20.2	1.0
	O	A:LEU203	4.9	17.7	1.0
	CG2	A:VAL255	5.0	15.3	1.0

Reference:

S.B.Silwal, B.Wamsley, Z.Wang, B.W.Gung, J.C.Nix, R.C.Page. Mutation of An Active Site-Adjacent Residue in Vim Indirectly Dictates Interactions with and Blunts Inhibition By D-Captopril. J.Inorg.Biochem. V. 271 12975 2025.
ISSN: ISSN 0162-0134
PubMed: 40513263
DOI: 10.1016/J.JINORGBIO.2025.112975

Page generated: Sat Aug 16 00:18:36 2025

Last articles

Mn in 9LJU
Mn in 9LJW
Mn in 9LJS
Mn in 9LJR
Mn in 9LJT
Mn in 9LJV
Mg in 9UA2
Mg in 9R96
Mg in 9VM1
Mg in 9P01

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