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Manganese in PDB 4o7x: Crystal Structure of Human ALKBH5 in Complex with MN2+

Protein crystallography data

The structure of Crystal Structure of Human ALKBH5 in Complex with MN2+, PDB code: 4o7x was solved by C.Feng, Z.Chen, Y.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.78
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 57.093, 57.093, 145.729, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 23.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human ALKBH5 in Complex with MN2+ (pdb code 4o7x). 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 Crystal Structure of Human ALKBH5 in Complex with MN2+, PDB code: 4o7x:

Manganese binding site 1 out of 1 in 4o7x

Go back to Manganese Binding Sites List in 4o7x
Manganese binding site 1 out of 1 in the Crystal Structure of Human ALKBH5 in Complex with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Human ALKBH5 in Complex with MN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn301

b:27.2
occ:0.70
OD1 A:ASP206 2.2 32.9 1.0
NE2 A:HIS266 2.2 27.0 1.0
O A:HOH475 2.2 39.8 1.0
NE2 A:HIS204 2.3 31.0 1.0
O A:HOH401 2.3 34.9 1.0
O A:HOH474 2.4 38.8 1.0
CE1 A:HIS266 3.0 29.2 1.0
CE1 A:HIS204 3.1 32.6 1.0
CG A:ASP206 3.2 31.4 1.0
CD2 A:HIS266 3.3 26.7 1.0
CD2 A:HIS204 3.4 30.2 1.0
OD2 A:ASP206 3.6 33.5 1.0
ND1 A:HIS266 4.2 27.7 1.0
O A:HOH452 4.3 43.2 1.0
ND1 A:HIS204 4.3 30.7 1.0
CG A:HIS266 4.4 25.2 1.0
CG A:HIS204 4.4 30.2 1.0
CB A:ASP206 4.5 29.7 1.0
N A:ASP206 4.8 23.8 1.0
CA A:ASP206 4.8 27.4 1.0
CD1 A:ILE201 5.0 45.2 1.0

Reference:

C.Feng, Y.Liu, G.Wang, Z.Deng, Q.Zhang, W.Wu, Y.Tong, C.Cheng, Z.Chen. Crystal Structures of Human Rna Demethylase ALKBH5 Reveal Basis For Substrate Recognition J.Biol.Chem. 2014.
ISSN: ESSN 1083-351X
DOI: 10.1074/JBC.M113.546168
Page generated: Sat Oct 5 20:41:42 2024

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