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Manganese in PDB 1z25: Structure of P.Furiosus Argonaute with Bound MN2+

Protein crystallography data

The structure of Structure of P.Furiosus Argonaute with Bound MN2+, PDB code: 1z25 was solved by F.V.Rivas, N.H.Tolia, J.J.Song, J.P.Aragon, J.Liu, G.J.Hannon, L.Joshua-Tor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.42 / 2.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 68.662, 105.108, 73.662, 90.00, 102.70, 90.00
R / Rfree (%) 21.5 / 27.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of P.Furiosus Argonaute with Bound MN2+ (pdb code 1z25). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Structure of P.Furiosus Argonaute with Bound MN2+, PDB code: 1z25:

Manganese binding site 1 out of 1 in 1z25

Go back to Manganese Binding Sites List in 1z25
Manganese binding site 1 out of 1 in the Structure of P.Furiosus Argonaute with Bound MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of P.Furiosus Argonaute with Bound MN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn771

b:46.5
occ:1.00
ND1 A:HIS745 2.1 39.8 1.0
O A:HOH788 2.4 43.6 1.0
O A:HOH781 2.4 39.5 1.0
OD2 A:ASP628 2.5 41.7 1.0
O A:HOH774 2.5 26.5 1.0
OD1 A:ASP558 2.8 62.5 1.0
CE1 A:HIS745 2.9 39.8 1.0
CG A:HIS745 3.3 39.8 1.0
CG A:ASP628 3.3 41.7 1.0
CG A:ASP558 3.3 62.5 1.0
OD2 A:ASP558 3.3 62.5 1.0
CB A:ASP628 3.6 41.7 1.0
CB A:HIS745 3.7 39.8 1.0
NE2 A:HIS745 4.1 39.8 1.0
OD1 A:ASP628 4.2 41.7 1.0
CD2 A:HIS745 4.3 39.8 1.0
CA A:HIS745 4.3 41.0 1.0
CB A:ASP558 4.6 62.5 1.0
O A:HOH778 4.7 39.1 1.0
O A:HOH908 4.8 47.8 1.0
NZ A:LYS657 4.9 56.6 1.0
O A:HOH935 5.0 51.5 1.0

Reference:

F.V.Rivas, N.H.Tolia, J.J.Song, J.P.Aragon, J.Liu, G.J.Hannon, L.Joshua-Tor. Purified ARGONAUTE2 and An Sirna Form Recombinant Human Risc. Nat.Struct.Mol.Biol. V. 12 340 2005.
ISSN: ISSN 1545-9993
PubMed: 15800637
DOI: 10.1038/NSMB918
Page generated: Tue Dec 15 03:58:35 2020

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