Calcium in PDB 4ghg: Structure of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.50 Ang Resolution

Enzymatic activity of Structure of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.50 Ang Resolution

All present enzymatic activity of Structure of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.50 Ang Resolution:
1.13.11.15;

Protein crystallography data

The structure of Structure of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.50 Ang Resolution, PDB code: 4ghg was solved by E.G.Kovaleva, J.D.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	45.86 / 1.50
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	110.540, 150.785, 96.276, 90.00, 90.00, 90.00
*R / R_free (%)*	12.7 / 16.1

Other elements in 4ghg:

The structure of Structure of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.50 Ang Resolution also contains other interesting chemical elements:

Iron	(Fe)	4 atoms
Chlorine	(Cl)	3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.50 Ang Resolution (pdb code 4ghg). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.50 Ang Resolution, PDB code: 4ghg:

Calcium binding site 1 out of 1 in 4ghg

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Calcium Binding Sites List in 4ghg

Calcium binding site 1 out of 1 in the Structure of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.50 Ang Resolution

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.50 Ang Resolution within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Ca402 b:32.6 occ:1.00	OE2	B:GLU185	2.2	36.5	1.0
	OD1	B:ASP184	2.4	18.4	1.0
	O	B:HOH501	2.9	28.2	1.0
	CD	B:GLU185	3.3	31.1	1.0
	CG	B:ASP184	3.3	17.3	1.0
	OD2	B:ASP184	3.6	16.8	1.0
	CG	B:GLU185	3.7	25.7	1.0
	OE1	B:GLU185	4.4	46.9	1.0
	NE2	B:HIS288	4.5	17.4	1.0
	CB	B:GLU185	4.6	21.7	1.0
	N	B:ASP184	4.6	14.9	1.0
	CB	B:ASP184	4.7	15.4	1.0
	N	B:GLU185	4.7	17.1	1.0
	CB	B:ASP183	4.8	14.9	1.0
	OD2	B:ASP183	4.9	18.2	1.0
	CG	B:ASP183	4.9	15.6	1.0
	C	B:ASP184	4.9	16.2	1.0
	CA	B:ASP184	4.9	15.4	1.0
	O	B:HOH749	5.0	33.1	1.0
	CD2	B:HIS288	5.0	15.2	1.0

Reference:

E.G.Kovaleva, J.D.Lipscomb. Structural Basis For the Role of Tyrosine 257 of Homoprotocatechuate 2,3-Dioxygenase in Substrate and Oxygen Activation. Biochemistry V. 51 8755 2012.
ISSN: ISSN 0006-2960
PubMed: 23066739
DOI: 10.1021/BI301115C

Page generated: Tue Jul 8 20:20:30 2025

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