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Sodium in PDB 2q0m: Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein

Enzymatic activity of Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein

All present enzymatic activity of Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein:
3.2.1.17;

Protein crystallography data

The structure of Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein, PDB code: 2q0m was solved by M.Razavet, V.Artero, C.Cavazza, Y.Oudart, J.C.Fontecilla-Camps, M.Fontecave, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.70
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.542, 79.542, 36.392, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 24.9

Other elements in 2q0m:

The structure of Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Manganese (Mn) 1 atom
Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein (pdb code 2q0m). 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 Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein, PDB code: 2q0m:

Sodium binding site 1 out of 1 in 2q0m

Go back to Sodium Binding Sites List in 2q0m
Sodium binding site 1 out of 1 in the Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Na131

b:26.8
occ:1.00
 O X:HOH211 2.3 28.4 1.0
O X:SER60 2.4 23.9 1.0
O X:ARG73 2.4 30.4 1.0
OG X:SER72 2.5 32.3 1.0
O X:CYS64 2.6 20.1 1.0
O X:HOH148 2.6 22.4 1.0
CB X:SER72 3.2 32.3 1.0
C X:ARG73 3.5 30.9 1.0
C X:SER60 3.6 22.9 1.0
C X:CYS64 3.6 20.2 1.0
N X:ARG73 3.8 32.1 1.0
CA X:ASN65 4.0 22.0 1.0
C X:SER72 4.0 32.5 1.0
CA X:SER60 4.2 21.7 1.0
CA X:ARG73 4.2 31.7 1.0
N X:ASN65 4.3 21.4 1.0
CA X:SER72 4.3 32.1 1.0
CB X:SER60 4.4 20.7 1.0
N X:ASN74 4.4 29.8 1.0
O X:ARG61 4.5 26.5 1.0
N X:CYS64 4.6 20.5 1.0
C X:ARG61 4.6 26.2 1.0
CA X:ASN74 4.6 29.1 1.0
N X:ARG61 4.6 24.3 1.0
O X:SER72 4.6 32.6 1.0
CB X:THR69 4.6 23.3 1.0
OD1 X:ASN65 4.7 25.9 1.0
O X:HOH140 4.7 15.1 1.0
CB X:ASN74 4.7 29.6 1.0
CA X:CYS64 4.7 20.1 1.0
CB X:ASN65 4.8 23.1 1.0
N X:ASP66 4.9 21.2 1.0
CA X:ARG61 4.9 25.6 1.0
N X:TRP62 4.9 25.5 1.0
OG1 X:THR69 4.9 21.8 1.0
O X:THR69 5.0 23.6 1.0

Reference:

M.Razavet, V.Artero, C.Cavazza, Y.Oudart, C.Lebrun, J.C.Fontecilla-Camps, M.Fontecave. Tricarbonylmanganese(I)-Lysozyme Complex: A Structurally Characterized Organometallic Protein Chem.Commun.(Camb.) 2805 2007.
ISSN: ESSN 1364-548X
PubMed: 17609782
DOI: 10.1039/B703887A
Page generated: Tue Dec 15 05:54:17 2020

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