Chlorine in PDB 8i2l: E. Coli Tryptophanyl-Trna Synthetase Bound with A Chemical Fragment at the Dimerization Interface

Enzymatic activity of E. Coli Tryptophanyl-Trna Synthetase Bound with A Chemical Fragment at the Dimerization Interface

All present enzymatic activity of E. Coli Tryptophanyl-Trna Synthetase Bound with A Chemical Fragment at the Dimerization Interface:
6.1.1.2;

Protein crystallography data

The structure of E. Coli Tryptophanyl-Trna Synthetase Bound with A Chemical Fragment at the Dimerization Interface, PDB code: 8i2l was solved by M.Xiang, H.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 1.95
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	61.617, 80.047, 78.28, 90, 105.69, 90
*R / R_free (%)*	19.9 / 22.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the E. Coli Tryptophanyl-Trna Synthetase Bound with A Chemical Fragment at the Dimerization Interface (pdb code 8i2l). 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 E. Coli Tryptophanyl-Trna Synthetase Bound with A Chemical Fragment at the Dimerization Interface, PDB code: 8i2l:

Chlorine binding site 1 out of 1 in 8i2l

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Chlorine Binding Sites List in 8i2l

Chlorine binding site 1 out of 1 in the E. Coli Tryptophanyl-Trna Synthetase Bound with A Chemical Fragment at the Dimerization Interface

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of E. Coli Tryptophanyl-Trna Synthetase Bound with A Chemical Fragment at the Dimerization Interface within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cl402 b:38.1 occ:1.00	CL1	B:CLW402	0.0	38.1	1.0
	C6	B:CLW402	1.7	33.1	1.0
	C5	B:CLW402	2.7	32.9	1.0
	C1	B:CLW402	2.7	32.4	1.0
	CA	A:GLY92	3.5	19.6	1.0
	O	A:GLY92	3.5	19.0	1.0
	C	A:GLY92	3.5	19.9	1.0
	N	A:LEU131	3.5	24.1	1.0
	CA	A:LEU131	3.6	24.6	1.0
	CB	A:LEU131	3.7	25.1	1.0
	CG1	A:VAL130	3.9	25.1	1.0
	C4	B:CLW402	4.0	32.1	1.0
	CE3	B:TRP93	4.0	25.9	1.0
	C2	B:CLW402	4.0	32.2	1.0
	C	A:VAL130	4.1	24.0	1.0
	OD2	A:ASP127	4.1	31.2	1.0
	CZ3	B:TRP93	4.1	26.9	1.0
	CD1	A:LEU131	4.1	25.8	1.0
	CB	A:VAL130	4.1	24.7	1.0
	N	A:TRP93	4.2	20.5	1.0
	CG	A:LEU131	4.5	25.4	1.0
	C3	B:CLW402	4.5	32.7	1.0
	O	A:VAL130	4.6	24.6	1.0
	O	A:ASP127	4.6	26.1	1.0
	CA	A:VAL130	4.7	25.0	1.0
	OD1	A:ASN96	4.8	27.1	1.0
	N	A:GLY92	4.8	19.4	1.0
	CG	A:ASP127	4.8	30.0	1.0
	CG	A:ASN96	4.9	26.0	1.0

Reference:

M.Xiang, K.Xia, B.Chen, Z.Luo, Y.Yu, L.Jiang, H.Zhou. An Asymmetric Structure of Bacterial Trprs Supports the Half-of-the-Sites Catalytic Mechanism and Facilitates Antimicrobial Screening To Be Published.

Page generated: Sun Jul 13 12:10:34 2025

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