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Magnesium in PDB 3ner: Structure of Human Type B Cytochrome B5

Protein crystallography data

The structure of Structure of Human Type B Cytochrome B5, PDB code: 3ner was solved by S.Terzyan, C.Zhang, M.Rivera, D.B.Benson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.24 / 1.45
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.316, 40.034, 58.744, 90.00, 98.61, 90.00
R / Rfree (%) 17.7 / 21.5

Other elements in 3ner:

The structure of Structure of Human Type B Cytochrome B5 also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Human Type B Cytochrome B5 (pdb code 3ner). 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 Structure of Human Type B Cytochrome B5, PDB code: 3ner:

Magnesium binding site 1 out of 1 in 3ner

Go back to Magnesium Binding Sites List in 3ner
Magnesium binding site 1 out of 1 in the Structure of Human Type B Cytochrome B5


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Type B Cytochrome B5 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg301

b:12.9
occ:1.00
O B:HOH88 2.1 19.9 1.0
O B:HOH93 2.1 12.2 1.0
O B:HOH90 2.1 17.6 1.0
O B:HOH95 2.1 17.0 1.0
O B:HOH91 2.2 18.7 1.0
O B:ASN16 3.9 13.4 1.0
O B:HOH107 4.0 23.9 1.0
O B:HOH176 4.1 33.7 1.0
O B:HOH127 4.2 25.5 1.0
O B:LEU47 4.3 11.7 1.0
O B:HOH215 4.4 36.4 1.0
CB B:LEU47 4.6 11.9 1.0
O B:HOH343 4.8 55.1 1.0
C B:LEU47 4.8 11.7 1.0

Reference:

S.Parthasarathy, A.Altuve, S.Terzyan, X.Zhang, K.Kuczera, M.Rivera, D.R.Benson. Accommodating A Non-Conservative Internal Mutation By Water-Mediated Hydrogen-Bonding Between Beta-Sheet Strands: A Comparison of Human and Rat Type B (Mitochondrial) Cytochrome B5 Biochemistry V. 50 5544 2011.
ISSN: ISSN 0006-2960
PubMed: 21574570
DOI: 10.1021/BI2004729
Page generated: Mon Aug 11 00:53:37 2025

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