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Manganese in PDB 1xms: E. Coli Reca in Complex with Mnamp-Pnp

Protein crystallography data

The structure of E. Coli Reca in Complex with Mnamp-Pnp, PDB code: 1xms was solved by C.E.Bell, X.Xing, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.49 / 2.10
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 100.700, 100.700, 81.900, 90.00, 90.00, 120.00
R / Rfree (%) 22.3 / 26.1

Manganese Binding Sites:

The binding sites of Manganese atom in the E. Coli Reca in Complex with Mnamp-Pnp (pdb code 1xms). 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 E. Coli Reca in Complex with Mnamp-Pnp, PDB code: 1xms:

Manganese binding site 1 out of 1 in 1xms

Go back to Manganese Binding Sites List in 1xms
Manganese binding site 1 out of 1 in the E. Coli Reca in Complex with Mnamp-Pnp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of E. Coli Reca in Complex with Mnamp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn701

b:64.9
occ:1.00
OG1 A:THR73 2.5 44.2 1.0
N3B A:ANP400 2.5 56.1 1.0
O A:HOH449 2.6 40.5 1.0
O2B A:ANP400 2.8 52.6 1.0
PG A:ANP400 3.2 54.5 1.0
O A:HOH417 3.2 54.3 1.0
PB A:ANP400 3.2 49.1 1.0
O1G A:ANP400 3.4 59.8 1.0
O3G A:ANP400 3.4 59.0 1.0
CB A:THR73 3.4 42.3 1.0
OD2 A:ASP144 3.9 37.3 1.0
N A:THR73 4.1 38.8 1.0
O1B A:ANP400 4.2 52.3 1.0
O A:HOH406 4.2 45.6 1.0
O2A A:ANP400 4.2 55.9 1.0
CA A:THR73 4.3 40.4 1.0
OD1 A:ASP144 4.4 35.0 1.0
O3A A:ANP400 4.4 53.9 1.0
O2G A:ANP400 4.5 59.8 1.0
CG2 A:THR73 4.5 46.4 1.0
CG A:ASP144 4.6 36.3 1.0
CE A:LYS72 4.6 30.1 1.0
O A:HOH504 4.8 63.3 1.0
OE1 A:GLU96 4.8 55.5 1.0
PA A:ANP400 4.9 53.9 1.0
NZ A:LYS72 4.9 31.2 1.0
O A:HOH490 5.0 57.5 1.0
CB A:LYS72 5.0 32.2 1.0

Reference:

X.Xing, C.E.Bell. Crystal Structures of Escherichia Coli Reca in Complex with Mgadp and Mnamp-Pnp(,). Biochemistry V. 43 16142 2004.
ISSN: ISSN 0006-2960
PubMed: 15610008
DOI: 10.1021/BI048165Y
Page generated: Tue Dec 15 03:58:09 2020

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