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Sodium in PDB 3qng: Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)]

Enzymatic activity of Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)]

All present enzymatic activity of Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)]:
3.2.1.17;

Protein crystallography data

The structure of Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)], PDB code: 3qng was solved by F.Zobi, B.Spingler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.12 / 1.55
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.343, 78.343, 36.546, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 21.7

Other elements in 3qng:

The structure of Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)] also contains other interesting chemical elements:

Rhenium (Re) 1 atom
Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)] (pdb code 3qng). 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 Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)], PDB code: 3qng:

Sodium binding site 1 out of 1 in 3qng

Go back to Sodium Binding Sites List in 3qng
Sodium binding site 1 out of 1 in the Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)]


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)] within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na220

b:29.6
occ:1.00
 O A:SER60 2.2 26.4 1.0
O A:HOH322 2.4 22.2 1.0
O A:ARG73 2.4 35.4 1.0
O A:HOH362 2.4 27.2 1.0
O A:CYS64 2.5 20.2 1.0
OG A:SER72 2.6 34.9 1.0
C A:SER60 3.3 23.7 1.0
CB A:SER72 3.4 24.3 1.0
C A:ARG73 3.4 35.4 1.0
C A:CYS64 3.5 18.9 1.0
CA A:SER60 4.0 17.8 1.0
CA A:ASN65 4.0 23.2 1.0
N A:ARG73 4.0 34.6 1.0
N A:ASN65 4.2 20.9 1.0
CB A:SER60 4.2 18.4 1.0
CA A:ARG73 4.3 28.0 1.0
N A:ASN74 4.3 23.4 1.0
C A:SER72 4.3 46.2 1.0
N A:CYS64 4.4 22.3 1.0
O A:ARG61 4.4 27.2 1.0
N A:ARG61 4.5 22.4 1.0
C A:ARG61 4.5 34.2 1.0
CA A:SER72 4.5 35.8 1.0
CA A:ASN74 4.6 19.6 1.0
CA A:CYS64 4.6 22.3 1.0
O A:HOH301 4.6 20.4 1.0
N A:ASP66 4.6 16.8 1.0
CB A:THR69 4.6 24.6 1.0
OD1 A:ASN65 4.7 25.3 1.0
CA A:ARG61 4.7 31.8 1.0
C A:ASN65 4.8 17.8 1.0
N A:TRP62 4.9 24.9 1.0
CB A:ASN74 4.9 27.3 1.0
CB A:ASN65 4.9 21.9 1.0
O A:SER72 4.9 39.9 1.0
N A:TRP63 5.0 20.2 1.0
OG1 A:THR69 5.0 21.6 1.0
OG A:SER60 5.0 21.0 1.0

Reference:

F.Zobi, B.Spingler. Post-Protein-Binding Reactivity and Modifications of the Fac-[Re(Co)3]+ Core Inorg.Chem. V. 51 1210 2012.
ISSN: ISSN 0020-1669
PubMed: 22229733
DOI: 10.1021/IC2023314
Page generated: Mon Oct 7 12:35:33 2024

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