Calcium in PDB 3bza: Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution

Enzymatic activity of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution

All present enzymatic activity of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution:
1.13.11.15;

Protein crystallography data

The structure of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution, PDB code: 3bza 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)*	28.82 / 1.70
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	110.502, 152.191, 96.278, 90.00, 90.00, 90.00
*R / R_free (%)*	17 / 19.7

Other elements in 3bza:

The structure of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution also contains other interesting chemical elements:

Manganese	(Mn)	4 atoms
Chlorine	(Cl)	4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution (pdb code 3bza). 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 Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution, PDB code: 3bza:

Calcium binding site 1 out of 1 in 3bza

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Calcium Binding Sites List in 3bza

Calcium binding site 1 out of 1 in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 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 Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.7 Ang Resolution within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Ca501 b:20.0 occ:1.00	OE2	B:GLU185	2.2	27.4	1.0
	OD1	B:ASP184	2.4	18.2	1.0
	O	B:HOH760	2.4	21.8	1.0
	CD	B:GLU185	3.3	27.1	1.0
	CG	B:ASP184	3.3	19.2	1.0
	OD2	B:ASP184	3.5	17.9	1.0
	CG	B:GLU185	3.7	23.9	1.0
	O	B:HOH831	4.1	42.7	1.0
	OE1	B:GLU185	4.4	29.6	1.0
	NE2	B:HIS288	4.5	19.4	1.0
	O	B:HOH1059	4.5	35.9	1.0
	N	B:ASP184	4.6	17.9	1.0
	CB	B:GLU185	4.6	21.5	1.0
	CB	B:ASP184	4.7	17.3	1.0
	N	B:GLU185	4.9	20.4	1.0
	CB	B:ASP183	4.9	17.6	1.0
	OD2	B:ASP183	4.9	21.3	1.0
	CD2	B:HIS288	5.0	17.1	1.0

Reference:

J.P.Emerson, E.G.Kovaleva, E.R.Farquhar, J.D.Lipscomb, L.Que. Swapping Metals in Fe- and Mn-Dependent Dioxygenases: Evidence For Oxygen Activation Without A Change in Metal Redox State. Proc.Natl.Acad.Sci.Usa V. 105 7347 2008.
ISSN: ISSN 0027-8424
PubMed: 18492808
DOI: 10.1073/PNAS.0711179105

Page generated: Tue Jul 8 11:16:53 2025

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