Calcium in PDB 7aq3: Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D

Enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D

All present enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D:
1.7.2.4;

Protein crystallography data

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D, PDB code: 7aq3 was solved by L.Zhang, E.Bill, P.M.H.Kroneck, O.Einsle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.33 / 1.64
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 69.664, 76.608, 109.087, 90, 93.26, 90
R / Rfree (%) 15.6 / 19.9

Other elements in 7aq3:

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D also contains other interesting chemical elements:

Potassium (K) 1 atom
Zinc (Zn) 2 atoms
Chlorine (Cl) 2 atoms
Copper (Cu) 8 atoms
Sodium (Na) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D (pdb code 7aq3). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D, PDB code: 7aq3:

Calcium binding site 1 out of 1 in 7aq3

Go back to Calcium Binding Sites List in 7aq3
Calcium binding site 1 out of 1 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1904

b:26.3
occ:0.62
O B:HOH2040 2.3 35.6 1.0
O B:MET267 2.4 39.0 1.0
OD1 B:ASN324 2.4 37.2 1.0
OE2 B:GLU259 2.4 37.9 1.0
O B:TYR256 2.5 37.6 1.0
OD2 B:ASP273 2.5 37.5 1.0
OD1 B:ASP273 2.6 35.8 1.0
OE1 B:GLU259 2.8 37.8 1.0
CG B:ASP273 2.9 40.9 1.0
CD B:GLU259 3.0 41.0 1.0
CG B:ASN324 3.4 39.8 1.0
C B:MET267 3.5 41.7 1.0
C B:TYR256 3.6 36.0 1.0
ND2 B:ASN324 4.0 38.3 1.0
CA B:MET268 4.3 43.2 1.0
N B:MET268 4.3 40.8 1.0
N B:ASN257 4.4 37.3 1.0
N B:SER258 4.4 37.7 1.0
CA B:ASN257 4.4 37.2 1.0
CA B:TYR256 4.5 39.6 1.0
CB B:ASP273 4.5 32.4 1.0
N B:ASN324 4.5 32.6 1.0
CG B:GLU259 4.5 35.6 1.0
OG B:SER258 4.5 42.7 1.0
CA B:MET267 4.5 40.2 1.0
O B:ASN270 4.5 48.3 1.0
CA B:ASN324 4.6 32.4 1.0
CB B:ASN324 4.6 34.8 1.0
C B:MET268 4.7 45.7 1.0
CB B:ASN270 4.7 45.1 1.0
N B:ASN270 4.8 44.3 1.0
N B:ARG269 4.8 44.1 1.0
C B:ASN257 4.9 44.0 1.0

Reference:

L.Zhang, E.Bill, P.M.H.Kroneck, O.Einsle. Histidine-Gated Proton-Coupled Electron Transfer to the Cu A Site of Nitrous Oxide Reductase. J.Am.Chem.Soc. 2020.
ISSN: ESSN 1520-5126
PubMed: 33377777
DOI: 10.1021/JACS.0C10057
Page generated: Sun Jan 24 09:37:00 2021

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