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Potassium in PDB 6c0h: Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA

Protein crystallography data

The structure of Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA, PDB code: 6c0h was solved by D.P.Cogan, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 75.84 / 1.90
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 39.990, 39.990, 303.353, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 25.1

Potassium Binding Sites:

The binding sites of Potassium atom in the Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA (pdb code 6c0h). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA, PDB code: 6c0h:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 6c0h

Go back to Potassium Binding Sites List in 6c0h
Potassium binding site 1 out of 2 in the Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K201

b:27.9
occ:1.00
O A:LEU29 2.5 26.8 1.0
O B:LEU45 2.7 27.2 1.0
O B:LEU43 2.8 30.8 1.0
O A:CYS26 2.9 24.8 1.0
O B:ALA42 2.9 24.9 1.0
O A:SER27 2.9 28.8 1.0
C B:LEU43 3.4 28.0 1.0
C A:SER27 3.5 28.4 1.0
C B:LEU45 3.7 31.4 1.0
CA B:LEU43 3.7 27.2 1.0
C A:LEU29 3.7 25.3 1.0
CA A:SER27 3.7 25.8 1.0
N B:LEU45 3.8 33.1 1.0
C A:CYS26 3.9 25.9 1.0
C B:ALA42 3.9 26.4 1.0
N A:LEU29 3.9 24.0 1.0
CA B:LEU45 4.1 34.8 1.0
CB B:LEU45 4.1 35.7 1.0
N B:LEU43 4.3 25.8 1.0
N A:SER27 4.3 25.4 1.0
N B:ALA44 4.3 30.1 1.0
CD A:PRO31 4.4 34.3 1.0
N A:LEU28 4.4 27.1 1.0
CA A:LEU29 4.4 25.3 1.0
N A:PRO31 4.4 32.4 1.0
CB B:GLU47 4.4 30.4 1.0
C B:ALA44 4.4 31.8 1.0
N B:GLU47 4.6 27.1 1.0
CA B:GLU47 4.7 30.1 1.0
C A:LEU28 4.7 28.5 1.0
C A:PRO30 4.7 28.8 1.0
N A:PRO30 4.7 27.9 1.0
CB A:LEU29 4.8 21.7 1.0
C B:HIS46 4.8 31.7 1.0
N B:HIS46 4.8 32.0 1.0
CG A:PRO31 4.9 37.5 1.0
CA B:ALA44 4.9 31.6 1.0
CA A:PRO30 4.9 29.7 1.0
CA A:PRO31 4.9 34.9 1.0
CB A:PRO31 5.0 36.5 1.0
CA A:LEU28 5.0 27.9 1.0
CB B:LEU43 5.0 27.0 1.0

Potassium binding site 2 out of 2 in 6c0h

Go back to Potassium Binding Sites List in 6c0h
Potassium binding site 2 out of 2 in the Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Lysinoalanine Synthase, Durn, From Duramycin Biosynthesis Bound to 1- DHA6ALA within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K202

b:27.6
occ:1.00
O B:LEU29 2.6 23.8 1.0
O A:LEU45 2.7 30.6 1.0
O B:SER27 2.8 30.2 1.0
O B:CYS26 2.8 24.2 1.0
O A:ALA42 2.9 23.6 1.0
O A:LEU43 2.9 25.7 1.0
C B:SER27 3.4 30.9 1.0
C A:LEU43 3.4 28.3 1.0
CA B:SER27 3.6 28.7 1.0
CA A:LEU43 3.7 27.2 1.0
C A:LEU45 3.7 30.3 1.0
C B:LEU29 3.8 25.8 1.0
N A:LEU45 3.8 29.1 1.0
C B:CYS26 3.9 26.1 1.0
C A:ALA42 3.9 25.2 1.0
N B:LEU29 4.0 23.6 1.0
CA A:LEU45 4.1 32.0 1.0
CB A:LEU45 4.1 31.7 1.0
N B:SER27 4.3 28.3 1.0
N A:LEU43 4.3 24.8 1.0
N B:LEU28 4.3 29.0 1.0
N A:ALA44 4.4 27.4 1.0
CA B:LEU29 4.4 25.6 1.0
C A:ALA44 4.4 29.1 1.0
CD B:PRO31 4.5 31.2 1.0
N B:PRO31 4.5 29.6 1.0
CB A:GLU47 4.5 32.5 1.0
N A:GLU47 4.7 26.9 1.0
C B:LEU28 4.8 28.3 1.0
C B:PRO30 4.8 28.8 1.0
CA A:GLU47 4.8 29.5 1.0
C A:HIS46 4.8 27.6 1.0
CB B:LEU29 4.9 24.8 1.0
N B:PRO30 4.9 27.5 1.0
N A:HIS46 4.9 31.4 1.0
CB B:PRO31 4.9 29.0 1.0
CA A:ALA44 4.9 28.2 1.0
CB B:SER27 4.9 33.9 1.0
CB A:LEU43 4.9 24.7 1.0
CA B:PRO31 4.9 29.8 1.0
CA B:PRO30 5.0 29.1 1.0
CG B:PRO31 5.0 33.9 1.0
CA B:LEU28 5.0 27.4 1.0

Reference:

L.An, D.P.Cogan, C.D.Navo, G.Jimenez-Oses, S.K.Nair, W.A.Van Der Donk. Substrate-Assisted Enzymatic Formation of Lysinoalanine in Duramycin. Nat. Chem. Biol. V. 14 928 2018.
ISSN: ESSN 1552-4469
PubMed: 30177849
DOI: 10.1038/S41589-018-0122-4
Page generated: Sat Aug 9 10:29:35 2025

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