Magnesium in PDB 4mv4: Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2

Enzymatic activity of Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2

All present enzymatic activity of Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2:
6.3.4.14; 6.4.1.2;

Protein crystallography data

The structure of Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2, PDB code: 4mv4 was solved by T.C.Broussard, S.Pakhomova, D.B.Neau, T.S.Champion, R.J.Bonnot, G.L.Waldrop, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	42.60 / 1.61
*Space group*	P 6₄
*Cell size a, b, c (Å), α, β, γ (°)*	85.344, 85.344, 104.217, 90.00, 90.00, 120.00
*R / R_free (%)*	15.4 / 18.4

Other elements in 4mv4:

The structure of Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2 (pdb code 4mv4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2, PDB code: 4mv4:

Magnesium binding site 1 out of 1 in 4mv4

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Magnesium Binding Sites List in 4mv4

Magnesium binding site 1 out of 1 in the Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg505 b:55.8 occ:1.00	O	A:HOH901	2.2	54.7	1.0
	OE2	A:GLU276	2.4	36.4	1.0
	HOG2	A:ACP501	2.4	93.4	1.0
	OE1	A:GLU288	2.6	65.7	1.0
	O1B	A:ACP501	2.6	0.8	1.0
	O2G	A:ACP501	2.6	77.9	1.0
	CD	A:GLU276	3.1	33.2	1.0
	OE1	A:GLU276	3.1	43.2	1.0
	HD22	A:ASN290	3.2	39.9	1.0
	OD1	A:ASN290	3.3	29.9	1.0
	CD	A:GLU288	3.6	57.0	1.0
	ND2	A:ASN290	3.9	33.2	1.0
	CG	A:ASN290	4.0	31.0	1.0
	PB	A:ACP501	4.0	0.1	1.0
	HB3	A:GLU288	4.0	46.4	1.0
	PG	A:ACP501	4.1	94.2	1.0
	OE2	A:GLU288	4.3	54.9	1.0
	CG	A:GLU276	4.5	27.9	1.0
	O2B	A:ACP501	4.5	0.1	1.0
	CG	A:GLU288	4.5	44.3	1.0
	HG3	A:GLU276	4.6	33.4	1.0
	HE1	A:HIS209	4.6	39.2	1.0
	HG2	A:GLU288	4.6	53.1	1.0
	CB	A:GLU288	4.6	38.6	1.0
	HD21	A:ASN290	4.6	39.9	1.0
	O	A:HOH884	4.7	34.4	1.0
	C3B	A:ACP501	4.7	66.9	1.0
	O3G	A:ACP501	4.7	71.2	1.0
	HH21	A:ARG292	4.8	31.6	1.0
	HB2	A:GLU288	4.8	46.4	1.0
	HH22	A:ARG292	4.9	31.6	1.0
	HG2	A:GLU276	5.0	33.4	1.0

Reference:

T.C.Broussard, S.Pakhomova, D.B.Neau, T.S.Champion, R.J.Bonnot, G.L.Waldrop. Structure of Biotin Carboxylase To Be Published.

Page generated: Mon Aug 19 23:23:22 2024

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