Chlorine in PDB 2x3c: ASAP1 Inactive Mutant E294Q, An Extracellular Toxic Zinc Metalloendopeptidase

Enzymatic activity of ASAP1 Inactive Mutant E294Q, An Extracellular Toxic Zinc Metalloendopeptidase

All present enzymatic activity of ASAP1 Inactive Mutant E294Q, An Extracellular Toxic Zinc Metalloendopeptidase:
3.4.24.39;

Protein crystallography data

The structure of ASAP1 Inactive Mutant E294Q, An Extracellular Toxic Zinc Metalloendopeptidase, PDB code: 2x3c was solved by X.Bogdanovic, G.J.Palm, R.K.Singh, W.Hinrichs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	57.60 / 1.99
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	101.958, 72.016, 54.996, 90.00, 109.78, 90.00
*R / R_free (%)*	17.2 / 21.4

Other elements in 2x3c:

The structure of ASAP1 Inactive Mutant E294Q, An Extracellular Toxic Zinc Metalloendopeptidase also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the ASAP1 Inactive Mutant E294Q, An Extracellular Toxic Zinc Metalloendopeptidase (pdb code 2x3c). 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 ASAP1 Inactive Mutant E294Q, An Extracellular Toxic Zinc Metalloendopeptidase, PDB code: 2x3c:

Chlorine binding site 1 out of 1 in 2x3c

Go back to

Chlorine Binding Sites List in 2x3c

Chlorine binding site 1 out of 1 in the ASAP1 Inactive Mutant E294Q, An Extracellular Toxic Zinc Metalloendopeptidase

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of ASAP1 Inactive Mutant E294Q, An Extracellular Toxic Zinc Metalloendopeptidase within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1343 b:37.5 occ:1.00	ZN	A:ZN1342	2.4	30.2	1.0
	NE2	A:HIS297	3.3	31.2	1.0
	CD2	A:HIS297	3.3	23.9	1.0
	NE2	A:HIS293	3.5	28.3	1.0
	CD2	A:HIS293	3.5	22.6	1.0
	OD1	A:ASP306	3.8	30.0	1.0
	CA	A:TYR261	3.9	23.0	1.0
	O	A:ALA260	4.0	25.9	1.0
	N	A:VAL262	4.3	24.2	1.0
	C	A:ALA260	4.4	25.2	1.0
	C	A:TYR261	4.4	23.9	1.0
	N	A:TYR261	4.4	22.1	1.0
	CG1	A:VAL262	4.5	24.2	1.0
	CE1	A:HIS297	4.6	21.9	1.0
	CA	A:GLN294	4.6	26.0	1.0
	CG	A:HIS297	4.6	21.1	1.0
	CG2	A:VAL262	4.7	25.6	1.0
	CE1	A:HIS293	4.7	24.6	1.0
	CB	A:GLN294	4.8	22.8	1.0
	CG	A:HIS293	4.8	27.7	1.0
	CG	A:ASP306	4.8	33.3	1.0
	CB	A:TYR261	5.0	25.2	1.0

Reference:

X.Bogdanovic, G.J.Palm, J.Schwenteit, R.K.Singh, B.K.Gudmundsdottir, W.Hinrichs. Structural Evidence of Intramolecular Propeptide Inhibition of the Aspzincin Metalloendopeptidase ASAP1. Febs Lett. V. 590 3280 2016.
ISSN: ISSN 0014-5793
PubMed: 27528449
DOI: 10.1002/1873-3468.12356

Page generated: Sat Jul 20 13:29:43 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF

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