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Magnesium in PDB 1nqf: Outer Membrane Cobalamin Transporter (Btub) From E. Coli, Methionine Substiution Construct For Se-Met Sad Phasing

Protein crystallography data

The structure of Outer Membrane Cobalamin Transporter (Btub) From E. Coli, Methionine Substiution Construct For Se-Met Sad Phasing, PDB code: 1nqf was solved by D.P.Chimento, A.K.Mohanty, R.J.Kadner, M.C.Wiener, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.70
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 81.614, 81.614, 226.653, 90.00, 90.00, 120.00
R / Rfree (%) 24.4 / 28.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Outer Membrane Cobalamin Transporter (Btub) From E. Coli, Methionine Substiution Construct For Se-Met Sad Phasing (pdb code 1nqf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Outer Membrane Cobalamin Transporter (Btub) From E. Coli, Methionine Substiution Construct For Se-Met Sad Phasing, PDB code: 1nqf:

Magnesium binding site 1 out of 1 in 1nqf

Go back to Magnesium Binding Sites List in 1nqf
Magnesium binding site 1 out of 1 in the Outer Membrane Cobalamin Transporter (Btub) From E. Coli, Methionine Substiution Construct For Se-Met Sad Phasing


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Outer Membrane Cobalamin Transporter (Btub) From E. Coli, Methionine Substiution Construct For Se-Met Sad Phasing within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg806

b:73.5
occ:1.00
CE1 A:HIS449 3.0 80.5 1.0
NE2 A:HIS449 3.4 88.1 1.0
ND1 A:HIS449 4.1 80.7 1.0
CD2 A:HIS449 4.7 71.6 1.0

Reference:

D.P.Chimento, A.K.Mohanty, R.J.Kadner, M.C.Wiener. Substrate-Induced Transmembrane Signaling in the Cobalamin Transporter Btub Nat.Struct.Biol. V. 10 394 2003.
ISSN: ISSN 1072-8368
PubMed: 12652322
DOI: 10.1038/NSB914
Page generated: Sun Aug 10 01:56:37 2025

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