Potassium in PDB 5h5a: MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified

The structure of MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified, PDB code: 5h5a was solved by S.Kawano, S.Quinbara, T.Endo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.26
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	42.868, 48.524, 130.126, 90.01, 91.50, 90.01
R / Rfree (%)	25.1 / 28.6

The binding sites of Potassium atom in the MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified (pdb code 5h5a). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified, PDB code: 5h5a:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in the MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified within 5.0Å range: probe atom residue distance (Å) B Occ A:K302 b:30.4 occ:1.00 O A:VAL37 2.6 26.3 1.0 OD1 A:ASN38 2.6 23.1 1.0 O A:PRO34 2.9 34.6 1.0 C A:VAL37 3.6 27.0 1.0 O A:LEU33 3.7 32.2 1.0 C A:PRO34 3.8 32.2 1.0 CG A:ASN38 3.9 24.0 1.0 CB A:LEU33 4.2 25.7 1.0 C A:LEU33 4.2 28.9 1.0 CA A:SER35 4.2 32.6 1.0 N A:ASN38 4.3 25.4 1.0 N A:VAL37 4.4 30.4 1.0 CA A:ASN38 4.4 24.9 1.0 C A:SER35 4.4 32.0 1.0 O A:SER35 4.4 27.9 1.0 N A:SER35 4.4 30.8 1.0 CA A:VAL37 4.5 30.0 1.0 CB A:ASN38 4.7 24.0 1.0 N A:PRO34 4.7 27.7 1.0 CA A:PRO34 4.8 29.3 1.0 ND2 A:ASN38 4.8 23.0 1.0 CA A:LEU33 4.9 28.0 1.0

Potassium binding site 2 out of 4 in the MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified within 5.0Å range: probe atom residue distance (Å) B Occ B:K302 b:32.0 occ:1.00 O B:VAL37 2.6 26.0 1.0 OD1 B:ASN38 2.7 24.1 1.0 O B:PRO34 2.8 31.1 1.0 C B:VAL37 3.6 25.9 1.0 O B:LEU33 3.6 31.0 1.0 C B:PRO34 3.7 30.9 1.0 CG B:ASN38 3.9 24.2 1.0 C B:LEU33 4.1 28.6 1.0 CB B:LEU33 4.1 29.9 1.0 CA B:SER35 4.2 33.5 1.0 N B:VAL37 4.3 29.4 1.0 N B:ASN38 4.3 24.9 1.0 CA B:ASN38 4.4 23.9 1.0 N B:SER35 4.4 32.6 1.0 C B:SER35 4.4 32.0 1.0 O B:SER35 4.5 30.3 1.0 CA B:VAL37 4.5 29.0 1.0 N B:PRO34 4.6 27.6 1.0 CA B:PRO34 4.7 28.6 1.0 CB B:ASN38 4.7 23.9 1.0 CA B:LEU33 4.8 29.4 1.0 ND2 B:ASN38 4.9 26.2 1.0

Potassium binding site 3 out of 4 in the MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified within 5.0Å range: probe atom residue distance (Å) B Occ C:K302 b:39.1 occ:1.00 O C:VAL37 2.6 32.5 1.0 O C:PRO34 2.7 39.3 1.0 OD1 C:ASN38 2.8 30.9 1.0 O C:LEU33 3.5 46.0 1.0 C C:VAL37 3.6 32.2 1.0 C C:PRO34 3.7 40.3 1.0 CG C:ASN38 4.0 29.3 1.0 C C:LEU33 4.1 41.1 1.0 CB C:LEU33 4.1 37.1 1.0 OD1 D:ASN185 4.2 80.5 1.0 CA C:SER35 4.2 41.6 1.0 N C:VAL37 4.3 34.1 1.0 N C:SER35 4.4 39.7 1.0 N C:ASN38 4.4 30.5 1.0 C C:SER35 4.4 40.6 1.0 CA C:ASN38 4.4 30.4 1.0 O C:SER35 4.5 35.7 1.0 CA C:VAL37 4.5 35.8 1.0 N C:PRO34 4.6 39.7 1.0 CA C:PRO34 4.7 40.7 1.0 CA C:LEU33 4.8 40.5 1.0 CB C:ASN38 4.8 31.3 1.0 ND2 C:ASN38 4.9 29.3 1.0 N C:TYR36 5.0 38.6 1.0

Potassium binding site 4 out of 4 in the MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of MDM12 From K. Lactis (1-239), Lys Residues Are Uniformly Dimethyl Modified within 5.0Å range: probe atom residue distance (Å) B Occ D:K302 b:36.1 occ:1.00 O D:VAL37 2.7 29.2 1.0 OD1 D:ASN38 2.8 30.3 1.0 O D:PRO34 2.8 39.8 1.0 O D:LEU33 3.5 41.4 1.0 C D:VAL37 3.7 27.9 1.0 C D:PRO34 3.8 35.6 1.0 CG D:ASN38 4.0 29.8 1.0 C D:LEU33 4.1 37.1 1.0 CB D:LEU33 4.1 33.8 1.0 CA D:SER35 4.3 35.0 1.0 N D:SER35 4.4 33.6 1.0 C D:SER35 4.4 33.2 1.0 CA D:ASN38 4.4 28.4 1.0 N D:ASN38 4.4 26.8 1.0 N D:VAL37 4.5 31.2 1.0 O D:SER35 4.5 33.6 1.0 N D:PRO34 4.6 35.3 1.0 CA D:VAL37 4.7 31.0 1.0 CA D:PRO34 4.7 37.4 1.0 CA D:LEU33 4.8 36.6 1.0 CB D:ASN38 4.8 29.2 1.0 ND2 D:ASN38 4.9 31.7 1.0

S.Kawano, Y.Tamura, R.Kojima, S.Bala, E.Asai, A.H.Michel, B.Kornmann, I.Riezman, H.Riezman, Y.Sakae, Y.Okamoto, T.Endo. Structure-Function Insights Into Direct Lipid Transfer Between Membranes By MMM1-MDM12 of Ermes J. Cell Biol. V. 217 959 2018.
ISSN: ESSN 1540-8140
PubMed: 29279306
DOI: 10.1083/JCB.201704119