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Potassium in PDB 2adq: Human Manganese Superoxide Dismutase

Enzymatic activity of Human Manganese Superoxide Dismutase

All present enzymatic activity of Human Manganese Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Human Manganese Superoxide Dismutase, PDB code: 2adq was solved by P.Quint, R.Reutzel, R.Mikulski, R.Mckenna, D.N.Silverman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.40
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 81.159, 81.159, 242.165, 90.00, 90.00, 120.00
R / Rfree (%) 21.7 / 24

Other elements in 2adq:

The structure of Human Manganese Superoxide Dismutase also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Human Manganese Superoxide Dismutase (pdb code 2adq). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Human Manganese Superoxide Dismutase, PDB code: 2adq:

Potassium binding site 1 out of 1 in 2adq

Go back to Potassium Binding Sites List in 2adq
Potassium binding site 1 out of 1 in the Human Manganese Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Manganese Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K200

b:37.9
occ:1.00
CD2 B:HIS2 3.5 27.0 1.0
NE2 B:HIS71 3.5 17.3 1.0
CB B:HIS2 3.7 28.7 1.0
CG B:HIS2 3.9 27.6 1.0
CA B:HIS2 4.0 30.6 1.0
O B:HOH220 4.0 44.0 1.0
O B:HOH219 4.1 48.4 1.0
N B:SER3 4.3 25.7 1.0
CD2 B:HIS71 4.4 14.4 1.0
CE1 B:HIS71 4.5 14.9 1.0
C B:HIS2 4.7 27.7 1.0
NE2 B:HIS2 4.7 27.2 1.0
O B:SER3 4.8 23.4 1.0

Reference:

P.Quint, R.Reutzel, R.Mikulski, R.Mckenna, D.N.Silverman. Crystal Structure of Nitrated Human Manganese Superoxide Dismutase: Mechanism of Inactivation. Free Radic.Biol.Med. V. 40 453 2006.
ISSN: ISSN 0891-5849
PubMed: 16443160
DOI: 10.1016/J.FREERADBIOMED.2005.08.045
Page generated: Sat Aug 9 03:06:50 2025

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