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Sodium in PDB 4n9r: X-Ray Structure of the Complex Between Hen Egg White Lysozyme and Pentacholrocarbonyliridate(III) (1 Day)

Enzymatic activity of X-Ray Structure of the Complex Between Hen Egg White Lysozyme and Pentacholrocarbonyliridate(III) (1 Day)

All present enzymatic activity of X-Ray Structure of the Complex Between Hen Egg White Lysozyme and Pentacholrocarbonyliridate(III) (1 Day):
3.2.1.17;

Protein crystallography data

The structure of X-Ray Structure of the Complex Between Hen Egg White Lysozyme and Pentacholrocarbonyliridate(III) (1 Day), PDB code: 4n9r was solved by A.A.Petruk, D.E.Bikiel, A.Vergara, A.Merlino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.45 / 1.55
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.319, 78.319, 37.049, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 19.4

Other elements in 4n9r:

The structure of X-Ray Structure of the Complex Between Hen Egg White Lysozyme and Pentacholrocarbonyliridate(III) (1 Day) also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms
Iridium (Ir) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the X-Ray Structure of the Complex Between Hen Egg White Lysozyme and Pentacholrocarbonyliridate(III) (1 Day) (pdb code 4n9r). 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 X-Ray Structure of the Complex Between Hen Egg White Lysozyme and Pentacholrocarbonyliridate(III) (1 Day), PDB code: 4n9r:

Sodium binding site 1 out of 1 in 4n9r

Go back to Sodium Binding Sites List in 4n9r
Sodium binding site 1 out of 1 in the X-Ray Structure of the Complex Between Hen Egg White Lysozyme and Pentacholrocarbonyliridate(III) (1 Day)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of X-Ray Structure of the Complex Between Hen Egg White Lysozyme and Pentacholrocarbonyliridate(III) (1 Day) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na204

b:20.1
occ:1.00
 O A:HOH322 2.3 19.6 1.0
O A:SER60 2.4 17.6 1.0
O A:HOH317 2.4 13.6 1.0
OG A:SER72 2.4 21.8 1.0
O A:ARG73 2.5 20.5 1.0
O A:CYS64 2.6 12.9 1.0
CB A:SER72 3.3 23.8 1.0
C A:SER60 3.5 15.6 1.0
C A:ARG73 3.6 19.0 1.0
C A:CYS64 3.6 11.1 1.0
CA A:ASN65 3.9 11.9 1.0
N A:ARG73 4.0 21.1 1.0
CA A:SER60 4.1 12.2 1.0
C A:SER72 4.1 24.9 1.0
N A:ASN65 4.2 11.8 1.0
O A:HOH377 4.3 34.1 1.0
CB A:SER60 4.3 13.5 1.0
CA A:SER72 4.4 24.1 1.0
CA A:ARG73 4.4 18.5 1.0
N A:ASN74 4.4 17.2 1.0
N A:CYS64 4.5 12.8 1.0
N A:ARG61 4.5 18.1 1.0
O A:ARG61 4.5 19.3 1.0
C A:ARG61 4.6 18.8 1.0
N A:ASP66 4.6 12.0 1.0
O A:SER72 4.6 25.4 1.0
CB A:THR69 4.6 17.3 1.0
CA A:ASN74 4.6 15.0 1.0
CL A:CL203 4.6 20.9 1.0
OD1 A:ASN65 4.6 18.5 1.0
CB A:ASN74 4.7 17.3 1.0
CA A:CYS64 4.7 13.5 1.0
CB A:ASN65 4.7 13.3 1.0
C A:ASN65 4.8 10.6 1.0
CA A:ARG61 4.8 19.5 1.0
N A:TRP62 4.8 15.8 1.0
O A:THR69 4.9 18.9 1.0

Reference:

A.A.Petruk, A.Vergara, D.Marasco, D.Bikiel, F.Doctorovich, D.A.Estrin, A.Merlino. Interaction Between Proteins and Ir Based Co Releasing Molecules: Mechanism of Adduct Formation and Co Release. Inorg.Chem. V. 53 10456 2014.
ISSN: ISSN 0020-1669
PubMed: 25215611
DOI: 10.1021/IC501498G
Page generated: Mon Oct 7 17:09:23 2024

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