Manganese in PDB 5b4c: Crystal Structure of H10N Mutant of Lpxh with Manganese

All present enzymatic activity of Crystal Structure of H10N Mutant of Lpxh with Manganese:
3.6.1.54;

The structure of Crystal Structure of H10N Mutant of Lpxh with Manganese, PDB code: 5b4c was solved by C.Okada, H.Wakabayashi, M.Yao, I.Tanaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.15 / 1.96
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.622, 97.999, 113.631, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 21.4

The binding sites of Manganese atom in the Crystal Structure of H10N Mutant of Lpxh with Manganese (pdb code 5b4c). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of H10N Mutant of Lpxh with Manganese, PDB code: 5b4c:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of H10N Mutant of Lpxh with Manganese


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 H10N Mutant of Lpxh with Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:20.1 occ:1.00 O A:HOH510 2.1 22.2 1.0 OD1 A:ASN79 2.1 21.1 1.0 OD2 A:ASP41 2.2 25.3 1.0 NE2 A:HIS114 2.3 22.4 1.0 O A:HOH481 2.3 23.3 1.0 ND1 A:HIS195 2.3 20.4 1.0 CG A:ASP41 3.1 22.0 1.0 CE1 A:HIS195 3.2 25.6 1.0 CG A:ASN79 3.2 25.0 1.0 CE1 A:HIS114 3.2 21.6 1.0 CD2 A:HIS114 3.3 23.5 1.0 CG A:HIS195 3.4 20.8 1.0 OD1 A:ASP41 3.4 22.1 1.0 ND2 A:ASN79 3.6 26.2 1.0 CB A:HIS195 3.8 23.7 1.0 CA A:HIS195 4.0 19.0 1.0 OD1 A:ASP8 4.1 21.8 1.0 O A:HOH428 4.2 25.7 1.0 CB A:ASP41 4.3 19.9 1.0 ND1 A:HIS114 4.3 21.3 1.0 NE2 A:HIS195 4.4 25.1 1.0 O A:HIS195 4.4 18.6 1.0 CG A:HIS114 4.4 20.3 1.0 N A:ASN79 4.5 21.2 1.0 CD2 A:HIS195 4.5 27.1 1.0 CB A:ASN79 4.5 22.3 1.0 C A:HIS195 4.7 19.6 1.0 CG A:ARG80 4.7 32.5 1.0 CB A:ASP116 4.9 22.1 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of H10N Mutant of Lpxh with Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of H10N Mutant of Lpxh with Manganese within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn301 b:21.4 occ:1.00 OD2 B:ASP41 2.1 25.8 1.0 OD1 B:ASN79 2.1 24.0 1.0 ND1 B:HIS195 2.3 18.9 1.0 NE2 B:HIS114 2.3 17.2 1.0 O B:HOH454 2.3 26.8 1.0 O B:HOH514 2.4 25.4 1.0 CE1 B:HIS195 3.1 24.8 1.0 CG B:ASP41 3.1 22.0 1.0 CG B:ASN79 3.2 24.6 1.0 CE1 B:HIS114 3.2 17.8 1.0 CD2 B:HIS114 3.3 17.3 1.0 CG B:HIS195 3.4 22.1 1.0 OD1 B:ASP41 3.5 21.9 1.0 ND2 B:ASN79 3.6 28.2 1.0 CB B:HIS195 3.8 19.0 1.0 CA B:HIS195 3.8 18.8 1.0 O B:HOH433 4.1 27.1 1.0 OD1 B:ASP8 4.1 26.5 1.0 NE2 B:HIS195 4.3 21.7 1.0 O B:HIS195 4.3 18.9 1.0 CB B:ASP41 4.3 19.6 1.0 ND1 B:HIS114 4.4 18.2 1.0 CD2 B:HIS195 4.4 21.6 1.0 N B:ASN79 4.4 21.5 1.0 CG B:HIS114 4.4 18.4 1.0 CB B:ASN79 4.5 24.3 1.0 C B:HIS195 4.6 20.6 1.0 CG B:ARG80 4.7 33.3 1.0 N B:HIS195 4.9 18.0 1.0

C.Okada, H.Wakabayashi, M.Kobayashi, A.Shinoda, I.Tanaka, M.Yao. Crystal Structures of the Udp-Diacylglucosamine Pyrophosphohydrase Lpxh From Pseudomonas Aeruginosa Sci Rep V. 6 32822 2016.
ISSN: ESSN 2045-2322
PubMed: 27609419
DOI: 10.1038/SREP32822