Zinc in PDB 5gov: Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain

The structure of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain, PDB code: 5gov was solved by M.Hu, J.Guo, S.Chen, Q.Hao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.13 / 2.33
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.439, 55.833, 219.388, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 23.6

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 11;

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain (pdb code 5gov). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 11 binding sites of Zinc where determined in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain, PDB code: 5gov:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 11 in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:31.4 occ:1.00 NE2 B:HIS282 2.1 24.9 1.0 NE2 B:HIS199 2.3 25.0 1.0 CE1 B:HIS282 3.0 24.0 1.0 CD2 B:HIS282 3.2 22.9 1.0 CD2 B:HIS199 3.2 24.8 1.0 CE1 B:HIS199 3.2 26.8 1.0 OG1 B:TPO89 3.6 36.6 1.0 O B:HOH595 4.0 37.3 1.0 ND1 B:HIS282 4.1 24.1 1.0 CG B:HIS282 4.3 24.8 1.0 O B:HOH593 4.3 24.1 1.0 ND1 B:HIS199 4.3 26.3 1.0 CG B:HIS199 4.3 24.5 1.0 NE2 B:HIS270 4.3 23.8 1.0 O B:HOH584 4.4 22.2 1.0 ZN B:ZN402 4.4 26.6 1.0 OE1 B:GLU50 4.5 24.1 1.0 CE1 B:HIS270 4.6 21.8 1.0 N B:TPO89 4.7 18.9 1.0 CB B:TPO89 4.8 36.8 1.0

Zinc binding site 2 out of 11 in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:26.6 occ:1.00 OD2 B:ASP269 1.9 21.6 1.0 OE1 B:GLU50 1.9 24.1 1.0 NE2 B:HIS270 2.1 23.8 1.0 OG1 B:TPO89 2.2 36.6 1.0 OE2 B:GLU50 2.4 24.3 1.0 CD B:GLU50 2.4 24.1 1.0 CD2 B:HIS270 2.8 18.9 1.0 CG B:ASP269 2.8 23.3 1.0 OD1 B:ASP269 3.1 20.8 1.0 CB B:TPO89 3.1 36.8 1.0 CE1 B:HIS270 3.2 21.8 1.0 N B:TPO89 3.4 18.9 1.0 CA B:TPO89 3.4 19.2 1.0 CG2 B:TPO89 3.5 37.0 1.0 O B:HOH504 3.7 25.7 1.0 CG B:GLU50 3.9 24.5 1.0 CG B:HIS270 4.0 22.5 1.0 ND1 B:HIS270 4.1 21.2 1.0 OG1 B:THR51 4.2 21.9 1.0 CB B:ASP269 4.2 23.1 1.0 C B:SER88 4.2 26.0 1.0 ZN B:ZN401 4.4 31.4 1.0 CD2 B:HIS199 4.4 24.8 1.0 N B:THR51 4.5 20.4 1.0 CA B:GLU50 4.6 21.4 1.0 CB B:GLU50 4.7 21.6 1.0 CA B:SER88 4.7 25.0 1.0 O B:SER88 4.9 23.5 1.0 NE2 B:HIS282 4.9 24.9 1.0 C B:TPO89 4.9 19.6 1.0 NE2 B:HIS199 5.0 25.0 1.0

Zinc binding site 3 out of 11 in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn403 b:71.0 occ:1.00 OD2 B:ASP108 2.1 61.7 1.0 OD2 B:ASP106 2.2 42.7 1.0 O B:HOH576 2.5 62.3 1.0 O B:HOH592 2.5 36.8 1.0 CG B:ASP106 3.0 43.0 1.0 CG B:ASP108 3.1 59.6 1.0 OD1 B:ASP106 3.2 47.3 1.0 CB B:ASP108 3.4 56.4 1.0 OD1 B:ASP108 4.1 60.2 1.0 N B:ASP108 4.3 49.9 1.0 CB B:ASP106 4.4 38.1 1.0 CA B:ASP108 4.5 53.2 1.0 O B:HOH605 4.8 45.8 1.0

Zinc binding site 4 out of 11 in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn404 b:56.5 occ:1.00 OE1 A:GLU104 2.4 37.0 1.0 OE1 B:GLU104 2.4 32.8 1.0 OE2 A:GLU104 2.6 41.4 1.0 OE2 B:GLU104 2.7 31.3 1.0 O B:HOH580 2.7 30.0 1.0 CD A:GLU104 2.8 39.8 1.0 CD B:GLU104 2.9 32.2 1.0 O A:HOH517 3.2 22.9 1.0 CG A:GLU104 4.4 36.5 1.0 NZ B:LYS336 4.4 59.4 1.0 CG B:GLU104 4.4 28.8 1.0 NZ A:LYS336 4.5 52.1 1.0 O B:HOH524 4.7 27.6 1.0 O A:HOH513 4.7 30.6 1.0 CB B:GLU104 5.0 25.2 1.0

Zinc binding site 5 out of 11 in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn405 b:32.4 occ:1.00 OD1 B:ASP103 2.0 38.4 1.0 OD2 A:ASP103 2.1 33.4 1.0 O B:HOH524 2.2 27.6 1.0 O A:HOH513 2.3 30.6 1.0 OD1 A:ASP103 2.5 36.2 1.0 OD2 B:ASP103 2.5 36.1 1.0 CG B:ASP103 2.6 35.7 1.0 CG A:ASP103 2.7 32.4 1.0 CG B:GLU104 3.9 28.8 1.0 CG A:GLU104 3.9 36.5 1.0 OE2 B:GLU104 4.0 31.3 1.0 O A:LEU100 4.0 34.3 1.0 O B:HOH572 4.0 28.7 1.0 CB B:ASP103 4.1 32.9 1.0 OE2 A:GLU104 4.1 41.4 1.0 O B:LEU100 4.1 35.2 1.0 CD A:GLU104 4.2 39.8 1.0 CB A:ASP103 4.2 26.4 1.0 CD B:GLU104 4.2 32.2 1.0 O A:HOH543 4.2 28.9 1.0 N B:GLU104 4.6 26.9 1.0 C B:ASP103 4.7 32.4 1.0 N A:GLU104 4.7 32.8 1.0 CA B:ASP103 4.7 31.9 1.0 CB A:GLU104 4.8 31.1 1.0 CB B:GLU104 4.8 25.2 1.0 C A:ASP103 4.8 25.6 1.0 N B:ASP103 4.8 32.4 1.0 CA A:ASP103 4.9 26.7 1.0 N A:ASP103 5.0 23.2 1.0 OE1 A:GLU104 5.0 37.0 1.0

Zinc binding site 6 out of 11 in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:27.7 occ:1.00 OD1 A:ASP269 1.9 18.9 1.0 OE1 A:GLU50 2.0 20.3 1.0 O2P A:TPO89 2.0 29.8 1.0 NE2 A:HIS270 2.1 22.0 1.0 OE2 A:GLU50 2.6 20.4 1.0 CD A:GLU50 2.6 19.5 1.0 CD2 A:HIS270 2.7 19.2 1.0 CG A:ASP269 2.9 19.8 1.0 P A:TPO89 3.0 28.1 1.0 CE1 A:HIS270 3.1 22.4 1.0 OD2 A:ASP269 3.2 19.2 1.0 CG2 A:TPO89 3.4 29.2 1.0 OG1 A:TPO89 3.4 32.6 1.0 O3P A:TPO89 3.6 28.0 1.0 CB A:TPO89 3.8 28.0 1.0 CG A:HIS270 3.9 19.3 1.0 N A:TPO89 4.0 29.5 1.0 CG A:GLU50 4.0 18.1 1.0 ND1 A:HIS270 4.0 20.5 1.0 OG1 A:THR51 4.1 26.1 1.0 CA A:TPO89 4.1 29.4 1.0 CB A:ASP269 4.2 18.1 1.0 O A:HOH520 4.4 23.2 1.0 O1P A:TPO89 4.4 28.5 1.0 N A:THR51 4.4 21.7 1.0 CA A:GLU50 4.6 20.7 1.0 NE2 A:HIS282 4.6 25.7 1.0 C A:SER88 4.7 23.3 1.0 CE1 A:HIS282 4.7 23.7 1.0 CB A:GLU50 4.8 19.2 1.0 C A:GLU50 5.0 19.2 1.0 ZN A:ZN403 5.0 31.9 1.0

Zinc binding site 7 out of 11 in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:29.0 occ:1.00 ZN A:ZN404 3.1 30.8 1.0 ZN A:ZN403 3.1 31.9 1.0 O1P A:TPO89 3.1 28.5 1.0 O3P A:TPO89 3.7 28.0 1.0 NE2 A:HIS199 3.9 33.0 1.0 CE1 A:HIS199 4.0 31.8 1.0 P A:TPO89 4.0 28.1 1.0 NE2 A:HIS282 4.8 25.7 1.0 O2P A:TPO89 4.9 29.8 1.0 O A:HOH555 4.9 26.2 1.0

Zinc binding site 8 out of 11 in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:31.9 occ:1.00 O3P A:TPO89 1.6 28.0 1.0 NE2 A:HIS282 2.0 25.7 1.0 CE1 A:HIS282 3.0 23.7 1.0 CD2 A:HIS282 3.0 23.3 1.0 P A:TPO89 3.0 28.1 1.0 ZN A:ZN402 3.1 29.0 1.0 O1P A:TPO89 3.6 28.5 1.0 OG1 A:TPO89 3.8 32.6 1.0 O2P A:TPO89 3.9 29.8 1.0 O A:HOH555 4.1 26.2 1.0 ND1 A:HIS282 4.1 23.2 1.0 CG A:HIS282 4.1 23.4 1.0 ZN A:ZN404 4.6 30.8 1.0 CB A:SER88 4.6 19.3 1.0 N A:TPO89 4.6 29.5 1.0 CA A:SER88 4.7 21.1 1.0 NE2 A:HIS199 4.8 33.0 1.0 NE2 A:HIS270 4.8 22.0 1.0 CE1 A:HIS199 4.9 31.8 1.0 ZN A:ZN401 5.0 27.7 1.0

Zinc binding site 9 out of 11 in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn404 b:30.8 occ:1.00 O1P A:TPO89 1.8 28.5 1.0 NE2 A:HIS199 2.0 33.0 1.0 O A:HOH571 2.3 47.5 1.0 CD2 A:HIS199 2.9 30.7 1.0 CE1 A:HIS199 3.0 31.8 1.0 ZN A:ZN402 3.1 29.0 1.0 P A:TPO89 3.2 28.1 1.0 O2P A:TPO89 3.4 29.8 1.0 O3P A:TPO89 4.0 28.0 1.0 CG A:HIS199 4.1 31.1 1.0 ND1 A:HIS199 4.1 29.6 1.0 OG1 A:TPO89 4.5 32.6 1.0 ZN A:ZN403 4.6 31.9 1.0 OD1 A:ASN133 4.6 35.6 1.0 OE2 A:GLU50 5.0 20.4 1.0 CE A:MET196 5.0 29.7 1.0

Zinc binding site 10 out of 11 in the Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Crystal Structure of Mcr-1, A Phosphoethanolamine Transferase, Extracellular Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn405 b:62.1 occ:1.00 O A:HOH582 2.5 35.8 1.0 NZ A:LYS187 3.8 44.5 1.0 O A:GLY124 4.1 33.0 1.0 OD1 A:ASP121 4.4 42.0 1.0 O A:VAL125 4.4 31.3 1.0 OG A:SER126 4.4 39.4 1.0 C A:GLY124 4.6 32.0 1.0 O A:ASP121 4.6 36.8 1.0 CA A:GLY124 4.8 32.6 1.0 CA A:SER126 4.8 33.7 1.0 C A:VAL125 4.9 29.6 1.0

M.Hu, J.Guo, Q.Cheng, Z.Yang, E.W.C.Chan, S.Chen, Q.Hao. Crystal Structure of Escherichia Coli Originated Mcr-1, A Phosphoethanolamine Transferase For Colistin Resistance Sci Rep V. 6 38793 2016.
ISSN: ESSN 2045-2322
DOI: 10.1038/SREP38793