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Magnesium in PDB 7z0w: E. Coli Nfsa Bound to Nadp+

Enzymatic activity of E. Coli Nfsa Bound to Nadp+

All present enzymatic activity of E. Coli Nfsa Bound to Nadp+:
1.5.1.38;

Protein crystallography data

The structure of E. Coli Nfsa Bound to Nadp+, PDB code: 7z0w was solved by S.A.White, A.Grainger, R.Parr, M.A.Day, D.Jarrom, A.Graziano, P.F.Searle, E.I.Hyde, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 81.45 / 2.06
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 96.766, 110.757, 112.25, 90, 103.84, 90
R / Rfree (%) 15.3 / 18.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E. Coli Nfsa Bound to Nadp+ (pdb code 7z0w). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the E. Coli Nfsa Bound to Nadp+, PDB code: 7z0w:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7z0w

Go back to Magnesium Binding Sites List in 7z0w
Magnesium binding site 1 out of 2 in the E. Coli Nfsa Bound to Nadp+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Nfsa Bound to Nadp+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg303

b:29.9
occ:1.00
O B:HOH533 2.0 28.5 1.0
O C:HOH434 2.0 30.2 1.0
O B:HOH462 2.1 29.9 1.0
O C:HOH564 2.1 28.4 1.0
O C:HOH562 2.1 24.8 1.0
O B:HOH508 2.2 26.6 1.0
O C:HOH449 3.9 40.1 1.0
O C:SER173 4.2 27.0 1.0
ND2 B:ASN179 4.4 27.3 1.0
O C:HOH475 4.4 25.4 1.0
OE2 B:GLU178 4.4 34.3 1.0
O C:HOH503 4.4 33.9 1.0
O C:HOH500 4.5 24.4 1.0
O C:HOH498 4.5 25.1 1.0
OD2 C:ASP185 4.6 33.9 1.0
CD B:GLU178 4.8 38.8 1.0
O C:HOH557 4.9 60.5 1.0

Magnesium binding site 2 out of 2 in 7z0w

Go back to Magnesium Binding Sites List in 7z0w
Magnesium binding site 2 out of 2 in the E. Coli Nfsa Bound to Nadp+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E. Coli Nfsa Bound to Nadp+ within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg302

b:32.8
occ:1.00
O C:HOH497 2.0 27.1 1.0
O B:HOH534 2.1 32.0 1.0
O C:HOH532 2.2 22.5 1.0
O C:HOH559 2.2 24.6 1.0
O B:HOH532 2.2 24.1 1.0
O B:HOH437 3.9 31.8 1.0
O B:SER173 4.1 23.4 1.0
O B:HOH464 4.2 28.4 1.0
ND2 C:ASN179 4.3 21.9 1.0
OD2 B:ASP185 4.3 25.3 1.0
O B:HOH445 4.4 24.2 1.0
O C:HOH581 4.5 44.0 1.0
O B:HOH465 4.5 31.6 1.0
O B:HOH489 4.5 26.6 1.0
OE2 C:GLU178 4.5 30.0 1.0
CD C:GLU178 4.9 34.2 1.0

Reference:

S.A.White, A.J.Christofferson, A.I.Grainger, M.A.Day, D.Jarrom, A.E.Graziano, P.F.Searle, E.I.Hyde. The 3D-Structure, Kinetics and Dynamics of the E. Coli Nitroreductase Nfsa with Nadp + Provide Glimpses of Its Catalytic Mechanism. Febs Lett. V. 596 2425 2022.
ISSN: ISSN 0014-5793
PubMed: 35648111
DOI: 10.1002/1873-3468.14413
Page generated: Thu Oct 3 16:12:55 2024

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