Sodium in PDB 3kgq: Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes

Enzymatic activity of Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes

All present enzymatic activity of Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes:
3.4.17.1;

Protein crystallography data

The structure of Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes, PDB code: 3kgq was solved by D.Fernandez, E.Boix, I.Pallares, F.X.Aviles, J.Vendrell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.24 / 1.70
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	40.604, 57.006, 60.604, 90.00, 102.04, 90.00
*R / R_free (%)*	18 / 20.4

Other elements in 3kgq:

The structure of Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes (pdb code 3kgq). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes, PDB code: 3kgq:

Sodium binding site 1 out of 1 in 3kgq

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Sodium Binding Sites List in 3kgq

Sodium binding site 1 out of 1 in the Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Na402 b:15.8 occ:1.00	N	A:LEU15	3.2	14.4	1.0
	O	A:HOH390	3.3	16.2	1.0
	O	A:HOH381	3.5	27.6	1.0
	ND1	A:HIS120	3.5	17.9	1.0
	CG	A:HIS120	3.6	17.0	1.0
	CB	A:LEU15	3.8	15.3	1.0
	CB	A:THR14	3.8	14.6	1.0
	CB	A:HIS120	3.8	17.1	1.0
	CA	A:ALA117	3.8	13.1	1.0
	CA	A:THR14	3.9	14.7	1.0
	C	A:THR14	4.1	14.6	1.0
	CA	A:LEU15	4.1	15.2	1.0
	CE1	A:HIS120	4.1	17.3	1.0
	CD2	A:HIS120	4.3	18.1	1.0
	O	A:PHE116	4.4	12.7	1.0
	CB	A:ALA117	4.4	13.2	1.0
	O	A:ALA117	4.5	13.2	1.0
	N	A:ALA117	4.5	12.8	1.0
	NE2	A:HIS120	4.5	17.2	1.0
	CG2	A:THR14	4.6	15.7	1.0
	C	A:ALA117	4.7	13.3	1.0
	C	A:PHE116	4.7	12.7	1.0
	OG1	A:THR14	4.8	15.2	1.0
	CD2	A:PHE116	4.9	13.3	1.0

Reference:

D.Fernandez, E.Boix, I.Pallares, F.X.Aviles, J.Vendrell. Structural and Functional Analysis of the Complex Between Citrate and the Zinc Peptidase Carboxypeptidase A Enzyme Res V.2011 28676 2011.
ISSN: ISSN 2090-0406
PubMed: 21804935
DOI: 10.4061/2011/128676

Page generated: Mon Oct 7 11:13:12 2024

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