Chlorine in PDB 5u0i: C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form

Enzymatic activity of C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form

All present enzymatic activity of C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form:
3.5.1.2;

Protein crystallography data

The structure of C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form, PDB code: 5u0i was solved by C.C.Pasquali, A.Gonzalez, S.M.G.Dias, A.L.B.Ambrosio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	38.09 / 1.42
*Space group*	P 4₃ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	75.290, 75.290, 88.310, 90.00, 90.00, 90.00
*R / R_free (%)*	14.4 / 18

Other elements in 5u0i:

The structure of C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form also contains other interesting chemical elements:

Sodium

(Na)

3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form (pdb code 5u0i). 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 C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form, PDB code: 5u0i:

Chlorine binding site 1 out of 1 in 5u0i

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Chlorine Binding Sites List in 5u0i

Chlorine binding site 1 out of 1 in the C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of C-Terminal Ankyrin Repeats From Human Kidney-Type Glutaminase (Kga) - Tetragonal Crystal Form within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl701 b:32.3 occ:1.00	NH2	A:ARG582	3.0	24.8	1.0
	N	A:LYS616	3.1	18.5	1.0
	O	A:HOH871	3.2	36.5	1.0
	CA	A:PRO615	3.8	17.4	1.0
	CB	A:LYS616	3.9	22.3	1.0
	CZ	A:ARG582	3.9	23.9	1.0
	C	A:PRO615	3.9	18.3	1.0
	CA	A:LYS616	4.0	17.6	1.0
	O	A:LYS616	4.0	17.3	1.0
	NH1	A:ARG582	4.0	20.9	1.0
	CG	A:LYS616	4.4	28.0	1.0
	CB	A:PRO615	4.5	17.1	1.0
	C	A:LYS616	4.5	16.5	1.0
	O	A:PHE614	4.6	22.7	1.0
	CE	A:LYS616	4.7	48.7	1.0
	OD1	A:ASN612	4.8	31.8	1.0
	O	A:HOH853	4.9	40.2	1.0
	N	A:PRO615	5.0	18.2	1.0

Reference:

C.C.Pasquali, Z.Islam, D.Adamoski, I.M.Ferreira, R.D.Righeto, J.Bettini, R.V.Portugal, W.W.Yue, A.Gonzalez, S.M.G.Dias, A.L.B.Ambrosio. The Origin and Evolution of Human Glutaminases and Their Atypical C-Terminal Ankyrin Repeats. J. Biol. Chem. V. 292 11572 2017.
ISSN: ESSN 1083-351X
PubMed: 28526749
DOI: 10.1074/JBC.M117.787291

Page generated: Sat Jul 12 09:11:07 2025

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