Chlorine in PDB 5czm: Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470

Enzymatic activity of Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470

All present enzymatic activity of Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470:
3.4.24.65;

Protein crystallography data

The structure of Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470, PDB code: 5czm was solved by C.Rouanet-Mehouas, L.Roselia, L.Devel, V.Dive, E.A.Stura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	28.45 / 1.30
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	68.970, 63.290, 35.910, 90.00, 90.00, 90.00
*R / R_free (%)*	14.5 / 17.4

Other elements in 5czm:

The structure of Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470 also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Bromine	(Br)	1 atom
Calcium	(Ca)	3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470 (pdb code 5czm). 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 A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470, PDB code: 5czm:

Chlorine binding site 1 out of 1 in 5czm

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Chlorine Binding Sites List in 5czm

Chlorine binding site 1 out of 1 in the Crystal Structure of A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470

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 A Mutated Catalytic Domain of Human MMP12 in Complex with RXP470 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl306 b:31.6 occ:1.00	CL1	A:R47306	0.0	31.6	1.0
	C1	A:R47306	1.7	26.0	1.0
	C2	A:R47306	2.7	22.3	1.0
	C3	A:R47306	2.7	25.2	1.0
	CE1	A:PHE248	3.2	18.2	1.0
	CD1	A:PHE248	3.3	18.1	1.0
	CG2	A:VAL243	3.4	26.8	1.0
	O	A:HOH567	3.5	28.3	1.0
	CG1	A:VAL243	3.6	26.9	1.0
	O	A:HOH474	3.9	28.3	1.0
	C6	A:R47306	4.0	19.2	1.0
	C4	A:R47306	4.0	24.3	1.0
	CB	A:VAL243	4.1	26.5	1.0
	O	A:LYS233	4.2	18.8	0.3
	O	A:LYS233	4.3	15.9	0.7
	C5	A:R47306	4.5	22.4	1.0
	CZ	A:PHE248	4.5	17.9	1.0
	O	A:HOH445	4.6	40.4	1.0
	CG	A:PHE248	4.7	18.1	1.0
	CD2	A:LEU214	4.7	15.5	1.0
	O	A:ARG249	4.7	16.3	1.0
	CA	A:VAL235	4.8	10.8	1.0
	CB	A:VAL235	4.9	11.2	1.0
	N	A:VAL235	4.9	11.3	1.0
	CG2	A:VAL235	4.9	12.1	1.0

Reference:

C.Rouanet-Mehouas, B.Czarny, F.Beau, E.Cassar-Lajeunesse, E.A.Stura, V.Dive, L.Devel. Zinc-Metalloproteinase Inhibitors: Evaluation of the Complex Role Played By the Zinc-Binding Group on Potency and Selectivity. J. Med. Chem. V. 60 403 2017.
ISSN: ISSN 1520-4804
PubMed: 27996256
DOI: 10.1021/ACS.JMEDCHEM.6B01420

Page generated: Sat Dec 12 11:36:58 2020

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