Zinc in PDB 4rzb: The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate, Soaked with Mercury

The structure of The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate, Soaked with Mercury, PDB code: 4rzb was solved by A.A.Fedorov, E.V.Fedorov, R.Marti-Arbona, F.M.Raushel, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.99 / 1.86
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.560, 141.831, 86.415, 90.00, 107.18, 90.00
R / Rfree (%)	16 / 17.6

The structure of The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate, Soaked with Mercury also contains other interesting chemical elements:

Mercury

(Hg)

6 atoms

The binding sites of Zinc atom in the The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate, Soaked with Mercury (pdb code 4rzb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate, Soaked with Mercury, PDB code: 4rzb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate, Soaked with Mercury


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate, Soaked with Mercury within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:13.7 occ:1.00 O A:HOH1040 2.0 12.3 1.0 NE2 A:HIS58 2.0 12.8 1.0 NE2 A:HIS56 2.1 13.2 1.0 NE2 A:HIS232 2.2 13.8 1.0 OD1 A:ASP320 2.5 14.4 1.0 CE1 A:HIS58 2.9 12.8 1.0 CE1 A:HIS56 3.0 13.1 1.0 CD2 A:HIS58 3.0 13.3 1.0 CD2 A:HIS56 3.1 12.9 1.0 CD2 A:HIS232 3.1 13.2 1.0 CE1 A:HIS232 3.2 14.2 1.0 CG A:ASP320 3.3 13.9 1.0 OD2 A:ASP320 3.6 13.5 1.0 NE2 A:HIS269 4.0 13.2 1.0 O A:HOH620 4.0 14.4 1.0 ND1 A:HIS58 4.0 13.3 1.0 CG A:HIS58 4.1 13.7 1.0 ND1 A:HIS56 4.1 12.8 1.0 N A:NFQ501 4.1 18.2 1.0 CG A:HIS56 4.2 12.7 1.0 ND1 A:HIS232 4.3 13.9 1.0 CG A:HIS232 4.3 13.4 1.0 O1 A:NFQ501 4.4 19.4 1.0 CF A:NFQ501 4.4 17.5 1.0 CA A:NFQ501 4.4 18.4 1.0 C A:NFQ501 4.5 19.1 1.0 NF A:NFQ501 4.5 17.1 1.0 CB A:ASP320 4.6 13.7 1.0 CE1 A:HIS269 4.7 12.9 1.0 CG1 A:VAL268 4.9 11.9 1.0

Zinc binding site 2 out of 2 in the The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate, Soaked with Mercury


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate, Soaked with Mercury within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:14.7 occ:1.00 NE2 B:HIS56 2.0 13.1 1.0 O B:HOH601 2.0 13.4 1.0 NE2 B:HIS58 2.0 14.2 1.0 NE2 B:HIS232 2.2 12.4 1.0 OD1 B:ASP320 2.5 13.5 1.0 CE1 B:HIS58 2.9 14.4 1.0 CE1 B:HIS56 2.9 13.3 1.0 CD2 B:HIS58 3.0 14.5 1.0 CD2 B:HIS56 3.1 12.5 1.0 CD2 B:HIS232 3.1 12.4 1.0 CE1 B:HIS232 3.1 13.2 1.0 CG B:ASP320 3.4 12.9 1.0 OD2 B:ASP320 3.6 12.7 1.0 ND1 B:HIS58 4.0 14.6 1.0 NE2 B:HIS269 4.0 12.3 1.0 ND1 B:HIS56 4.1 12.8 1.0 O B:HOH620 4.1 14.4 1.0 CG B:HIS58 4.1 14.8 1.0 CG B:HIS56 4.2 12.4 1.0 N B:NFQ501 4.2 18.2 1.0 ND1 B:HIS232 4.2 13.7 1.0 CG B:HIS232 4.3 13.3 1.0 CA B:NFQ501 4.4 18.9 1.0 CF B:NFQ501 4.5 17.5 1.0 O1 B:NFQ501 4.5 19.3 1.0 C B:NFQ501 4.5 19.4 1.0 NF B:NFQ501 4.5 16.8 1.0 CB B:ASP320 4.7 12.6 1.0 CE1 B:HIS269 4.8 11.8 1.0 CG1 B:VAL268 4.9 11.9 1.0

A.A.Fedorov, R.Marti-Arbona, V.V.Nemmara, D.Hitchcock, E.V.Fedorov, S.C.Almo, F.M.Raushel. Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa. Biochemistry V. 54 890 2015.
ISSN: ISSN 0006-2960
PubMed: 25559274
DOI: 10.1021/BI501299Y