Chlorine in PDB 3v13: Bovine Trypsin Variant X(TRIPLEGLU217PHE227) in Complex with Small Molecule Inhibitor

Enzymatic activity of Bovine Trypsin Variant X(TRIPLEGLU217PHE227) in Complex with Small Molecule Inhibitor

All present enzymatic activity of Bovine Trypsin Variant X(TRIPLEGLU217PHE227) in Complex with Small Molecule Inhibitor:
3.4.21.4;

Protein crystallography data

The structure of Bovine Trypsin Variant X(TRIPLEGLU217PHE227) in Complex with Small Molecule Inhibitor, PDB code: 3v13 was solved by A.Tziridis, P.Neumann, P.Kolenko, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	70.89 / 1.63
*Space group*	P 6₅
*Cell size a, b, c (Å), α, β, γ (°)*	81.813, 81.813, 63.865, 90.00, 90.00, 120.00
*R / R_free (%)*	14.6 / 17.5

Other elements in 3v13:

The structure of Bovine Trypsin Variant X(TRIPLEGLU217PHE227) in Complex with Small Molecule Inhibitor also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Bovine Trypsin Variant X(TRIPLEGLU217PHE227) in Complex with Small Molecule Inhibitor (pdb code 3v13). 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 Bovine Trypsin Variant X(TRIPLEGLU217PHE227) in Complex with Small Molecule Inhibitor, PDB code: 3v13:

Chlorine binding site 1 out of 1 in 3v13

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Chlorine Binding Sites List in 3v13

Chlorine binding site 1 out of 1 in the Bovine Trypsin Variant X(TRIPLEGLU217PHE227) in Complex with Small Molecule Inhibitor

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Bovine Trypsin Variant X(TRIPLEGLU217PHE227) in Complex with Small Molecule Inhibitor within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl487 b:25.3 occ:0.80	O	A:HOH1398	2.3	31.9	1.0
	N	A:ASP153	3.3	11.7	1.0
	N	A:VAL154	3.6	9.8	1.0
	CG2	A:VAL154	3.8	11.2	1.0
	CB	A:ASP153	3.9	12.2	1.0
	O	A:HOH1297	3.9	39.3	1.0
	CB	A:PRO152	4.0	12.1	1.0
	CA	A:PRO152	4.0	12.2	1.0
	CA	A:ASP153	4.0	11.8	1.0
	NZ	A:LYS156	4.1	13.9	1.0
	O	A:HOH1399	4.1	32.3	1.0
	C	A:PRO152	4.1	11.9	1.0
	CE	A:LYS156	4.2	13.5	1.0
	C	A:ASP153	4.3	10.8	1.0
	CB	A:VAL154	4.6	9.4	1.0
	O	A:HOH1119	4.6	43.9	1.0
	CG	A:ASP153	4.6	15.4	1.0
	CA	A:VAL154	4.6	10.0	1.0
	OD2	A:ASP153	4.6	22.7	1.0
	CG1	A:VAL154	4.7	9.8	1.0
	O	A:VAL154	4.9	9.5	1.0

Reference:

A.Tziridis, D.Rauh, P.Neumann, P.Kolenko, A.Menzel, U.Brauer, C.Ursel, P.Steinmetzer, J.Sturzebecher, A.Schweinitz, T.Steinmetzer, M.T.Stubbs. Correlating Structure and Ligand Affinity in Drug Discovery: A Cautionary Tale Involving Second Shell Residues. Biol.Chem. V. 395 891 2014.
ISSN: ISSN 1431-6730
PubMed: 25003390
DOI: 10.1515/HSZ-2014-0158

Page generated: Sat Dec 12 10:16:29 2020

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