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Sodium in PDB 6gm6: [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii,Variant E141Q

Enzymatic activity of [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii,Variant E141Q

All present enzymatic activity of [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii,Variant E141Q:
1.18.99.1;

Protein crystallography data

The structure of [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii,Variant E141Q, PDB code: 6gm6 was solved by J.Duan, V.Engelbrecht, J.Esselborn, E.Hofmann, M.Winkler, T.Happe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.09 / 1.61
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.790, 70.790, 155.030, 90.00, 90.00, 120.00
R / Rfree (%) 16.4 / 19.9

Other elements in 6gm6:

The structure of [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii,Variant E141Q also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii,Variant E141Q (pdb code 6gm6). 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 [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii,Variant E141Q, PDB code: 6gm6:

Sodium binding site 1 out of 1 in 6gm6

Go back to Sodium Binding Sites List in 6gm6
Sodium binding site 1 out of 1 in the [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii,Variant E141Q


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii,Variant E141Q within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na603

b:29.1
occ:1.00
 O A:HOH787 2.4 27.2 1.0
O A:HOH797 2.4 30.1 1.0
O A:HOH854 2.4 40.0 1.0
O A:HOH753 2.4 29.4 1.0
O A:HOH1103 2.4 35.2 1.0
O A:TRP276 2.4 18.6 1.0
C A:TRP276 3.6 16.6 1.0
O A:HOH1164 3.6 43.6 1.0
N A:GLY285 3.8 25.8 1.0
OD1 A:ASP277 4.0 20.8 1.0
CA A:ASP277 4.0 15.7 1.0
O A:HOH1054 4.0 40.2 1.0
N A:ASP277 4.2 15.3 1.0
CA A:SER284 4.3 28.6 1.0
O A:GLY283 4.4 38.1 1.0
O A:GLY285 4.4 21.6 1.0
OE1 A:GLU275 4.4 43.1 1.0
CB A:GLU275 4.5 27.5 1.0
C A:SER284 4.5 26.8 1.0
O A:HOH742 4.6 38.7 1.0
CA A:GLY285 4.7 22.8 1.0
CG A:ASP277 4.7 19.6 1.0
N A:TRP276 4.8 17.1 1.0
CA A:TRP276 4.8 18.3 1.0
N A:ASN278 4.8 18.7 1.0
CB A:ASP277 4.9 16.9 1.0
C A:ASP277 4.9 18.2 1.0
C A:GLY285 4.9 22.1 1.0
O A:HOH1126 5.0 49.8 1.0

Reference:

J.Duan, M.Senger, J.Esselborn, V.Engelbrecht, F.Wittkamp, U.P.Apfel, E.Hofmann, S.T.Stripp, T.Happe, M.Winkler. Crystallographic and Spectroscopic Assignment of the Proton Transfer Pathway in [Fefe]-Hydrogenases. Nat Commun V. 9 4726 2018.
ISSN: ESSN 2041-1723
PubMed: 30413719
DOI: 10.1038/S41467-018-07140-X
Page generated: Tue Dec 15 12:17:51 2020

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