Chlorine in PDB 4gg2: The Crystal Structure of Glutamate-Bound Human Gamma- Glutamyltranspeptidase 1

Enzymatic activity of The Crystal Structure of Glutamate-Bound Human Gamma- Glutamyltranspeptidase 1

All present enzymatic activity of The Crystal Structure of Glutamate-Bound Human Gamma- Glutamyltranspeptidase 1:
2.3.2.2; 3.4.19.13; 3.4.19.14;

Protein crystallography data

The structure of The Crystal Structure of Glutamate-Bound Human Gamma- Glutamyltranspeptidase 1, PDB code: 4gg2 was solved by M.B.West, Y.Chen, S.Wickham, A.Heroux, K.Cahill, M.H.Hanigan, B.H.M.Mooers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	43.98 / 2.21
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	105.717, 126.753, 104.629, 90.00, 90.00, 90.00
*R / R_free (%)*	14 / 18.3

Other elements in 4gg2:

The structure of The Crystal Structure of Glutamate-Bound Human Gamma- Glutamyltranspeptidase 1 also contains other interesting chemical elements:

Iodine

(I)

10 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Crystal Structure of Glutamate-Bound Human Gamma- Glutamyltranspeptidase 1 (pdb code 4gg2). 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 The Crystal Structure of Glutamate-Bound Human Gamma- Glutamyltranspeptidase 1, PDB code: 4gg2:

Chlorine binding site 1 out of 1 in 4gg2

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Chlorine Binding Sites List in 4gg2

Chlorine binding site 1 out of 1 in the The Crystal Structure of Glutamate-Bound Human Gamma- Glutamyltranspeptidase 1

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of Glutamate-Bound Human Gamma- Glutamyltranspeptidase 1 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cl607 b:26.0 occ:0.97	H	B:HIS383	2.4	32.3	1.0
	HZ2	B:LYS562	2.6	39.6	1.0
	HE22	B:GLN545	2.6	31.6	1.0
	HA	B:ALA382	2.6	33.2	1.0
	HB3	A:ASP46	2.9	37.7	1.0
	HD3	B:LYS562	2.9	35.6	1.0
	OD2	A:ASP46	3.0	31.2	1.0
	HB2	B:ALA472	3.1	35.8	1.0
	HG11	B:VAL543	3.2	32.3	1.0
	NE2	B:GLN545	3.2	26.3	1.0
	N	B:HIS383	3.3	26.9	1.0
	HE21	B:GLN545	3.3	31.6	1.0
	NZ	B:LYS562	3.3	33.0	1.0
	HB1	B:ALA472	3.4	35.8	1.0
	HZ1	B:LYS562	3.4	39.6	1.0
	CA	B:ALA382	3.5	27.6	1.0
	CB	A:ASP46	3.5	31.4	1.0
	HG12	B:VAL543	3.5	32.3	1.0
	HB2	A:ASP46	3.5	37.7	1.0
	HB	B:VAL543	3.6	29.0	1.0
	HB3	B:ALA382	3.6	29.2	1.0
	CD	B:LYS562	3.6	29.6	1.0
	CB	B:ALA472	3.7	29.8	1.0
	CG	A:ASP46	3.7	31.7	1.0
	CG1	B:VAL543	3.7	26.9	1.0
	HD2	B:LYS562	3.8	35.6	1.0
	C	B:ALA382	3.9	29.6	1.0
	CE	B:LYS562	4.0	25.8	1.0
	HZ3	B:LYS562	4.0	39.6	1.0
	CB	B:ALA382	4.0	24.3	1.0
	HB3	B:ALA472	4.0	35.8	1.0
	O	B:HIS383	4.1	26.1	1.0
	CB	B:VAL543	4.2	24.1	1.0
	HB1	B:ALA382	4.2	29.2	1.0
	HE2	B:LYS562	4.3	30.9	1.0
	HB3	B:HIS383	4.3	29.8	1.0
	O	B:THR381	4.3	25.3	1.0
	O	B:HOH711	4.3	24.9	1.0
	CA	B:HIS383	4.4	23.2	1.0
	CD	B:GLN545	4.4	24.6	1.0
	HG13	B:VAL543	4.6	32.3	1.0
	N	B:ALA382	4.6	25.2	1.0
	C	B:HIS383	4.7	24.2	1.0
	HG22	B:VAL543	4.7	33.4	1.0
	CB	B:HIS383	4.8	24.8	1.0
	O	B:VAL543	4.8	26.9	1.0
	HE3	B:LYS562	4.9	30.9	1.0
	OE1	B:GLN545	4.9	26.2	1.0
	OD1	A:ASP46	4.9	26.9	1.0
	CA	A:ASP46	4.9	31.0	1.0
	HB2	B:ALA382	4.9	29.2	1.0
	C	B:THR381	4.9	24.8	1.0
	H	B:ALA472	4.9	32.3	1.0
	CG2	B:VAL543	4.9	27.8	1.0
	CG	B:LYS562	4.9	28.6	1.0
	HB2	B:HIS383	4.9	29.8	1.0
	HG23	B:VAL543	5.0	33.4	1.0
	HB3	B:LYS562	5.0	37.9	1.0
	CA	B:ALA472	5.0	30.5	1.0

Reference:

M.B.West, Y.Chen, S.Wickham, A.Heroux, K.Cahill, M.H.Hanigan, B.H.Mooers. Novel Insights Into Eukaryotic Gamma-Glutamyltranspeptidase 1 From the Crystal Structure of the Glutamate-Bound Human Enzyme. J.Biol.Chem. V. 288 31902 2013.
ISSN: ISSN 0021-9258
PubMed: 24047895
DOI: 10.1074/JBC.M113.498139

Page generated: Sat Dec 12 10:39:29 2020

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