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

The structure of The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate, PDB code: 4rdv 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)	45.51 / 2.08
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	304.047, 67.248, 98.231, 90.00, 91.50, 90.00
R / Rfree (%)	14.4 / 18.3

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 (pdb code 4rdv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 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, PDB code: 4rdv:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:20.2 occ:0.71 O A:HOH601 1.9 16.1 1.0 NE2 A:HIS58 2.0 12.0 1.0 NE2 A:HIS56 2.0 13.2 1.0 NE2 A:HIS232 2.1 16.1 1.0 OD1 A:ASP320 2.7 14.9 1.0 CE1 A:HIS56 2.9 13.0 1.0 CE1 A:HIS58 2.9 12.5 1.0 CD2 A:HIS58 3.0 10.6 1.0 CD2 A:HIS232 3.1 13.3 1.0 CE1 A:HIS232 3.1 16.8 1.0 CD2 A:HIS56 3.1 10.8 1.0 CG A:ASP320 3.5 17.1 1.0 OD2 A:ASP320 3.6 20.6 1.0 NE2 A:HIS269 4.0 20.8 1.0 ND1 A:HIS58 4.0 18.7 1.0 ND1 A:HIS56 4.0 12.5 1.0 CG A:HIS58 4.1 9.8 1.0 O A:HOH652 4.1 14.0 1.0 CG A:HIS56 4.2 9.9 1.0 ND1 A:HIS232 4.2 19.0 1.0 N A:NFQ501 4.2 17.1 1.0 CG A:HIS232 4.2 17.1 1.0 CF A:NFQ501 4.4 16.5 1.0 CA A:NFQ501 4.5 17.0 1.0 NF A:NFQ501 4.5 18.6 1.0 O1 A:NFQ501 4.5 15.7 1.0 C A:NFQ501 4.6 19.3 1.0 CE1 A:HIS269 4.7 16.2 1.0 CG1 A:VAL268 4.7 9.9 1.0 CB A:ASP320 4.7 16.8 1.0 CD2 A:HIS269 5.0 18.3 1.0

Zinc binding site 2 out of 4 in the The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate


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 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:21.0 occ:0.85 O B:HOH601 2.0 18.5 1.0 NE2 B:HIS58 2.0 18.7 1.0 NE2 B:HIS56 2.1 12.1 1.0 NE2 B:HIS232 2.2 19.0 1.0 OD1 B:ASP320 2.6 14.8 1.0 CD2 B:HIS58 3.0 11.5 1.0 CE1 B:HIS56 3.0 10.4 1.0 CE1 B:HIS58 3.0 21.1 1.0 CD2 B:HIS232 3.2 11.4 1.0 CD2 B:HIS56 3.2 10.3 1.0 CE1 B:HIS232 3.2 16.9 1.0 CG B:ASP320 3.4 19.1 1.0 OD2 B:ASP320 3.6 17.4 1.0 N B:NFQ501 3.9 34.6 1.0 O B:HOH616 4.0 19.6 1.0 NE2 B:HIS269 4.0 17.3 1.0 ND1 B:HIS58 4.1 17.5 1.0 CG B:HIS58 4.1 15.3 1.0 ND1 B:HIS56 4.1 10.4 1.0 CG B:HIS56 4.2 11.4 1.0 ND1 B:HIS232 4.3 18.8 1.0 CG B:HIS232 4.3 16.3 1.0 CA B:NFQ501 4.3 33.9 1.0 NF B:NFQ501 4.3 30.0 1.0 CF B:NFQ501 4.4 31.4 1.0 C B:NFQ501 4.4 30.1 1.0 O1 B:NFQ501 4.5 24.5 1.0 CB B:ASP320 4.7 13.0 1.0 CE1 B:HIS269 4.8 18.0 1.0 CG1 B:VAL268 4.9 10.1 1.0

Zinc binding site 3 out of 4 in the The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn502 b:19.9 occ:0.81 NE2 C:HIS56 2.0 10.3 1.0 NE2 C:HIS58 2.0 14.9 1.0 O C:HOH601 2.1 11.1 1.0 NE2 C:HIS232 2.1 14.4 1.0 OD1 C:ASP320 2.7 17.6 1.0 CE1 C:HIS58 2.9 18.5 1.0 CE1 C:HIS56 2.9 12.6 1.0 CD2 C:HIS58 3.0 15.0 1.0 CD2 C:HIS56 3.1 12.3 1.0 CD2 C:HIS232 3.1 10.7 1.0 CE1 C:HIS232 3.1 15.5 1.0 CG C:ASP320 3.5 23.8 1.0 OD2 C:ASP320 3.7 19.8 1.0 NE2 C:HIS269 4.0 18.5 1.0 ND1 C:HIS58 4.0 15.2 1.0 ND1 C:HIS56 4.1 10.8 1.0 CG C:HIS58 4.1 15.7 1.0 O C:HOH619 4.1 15.2 1.0 N C:NFQ501 4.1 23.2 1.0 CG C:HIS56 4.2 13.9 1.0 ND1 C:HIS232 4.2 11.3 1.0 CG C:HIS232 4.2 11.0 1.0 O1 C:NFQ501 4.4 19.5 1.0 NF C:NFQ501 4.4 29.8 1.0 CA C:NFQ501 4.4 27.3 1.0 CF C:NFQ501 4.5 31.6 1.0 C C:NFQ501 4.5 25.1 1.0 CE1 C:HIS269 4.7 17.3 1.0 CB C:ASP320 4.7 18.2 1.0 CG1 C:VAL268 4.8 9.7 1.0

Zinc binding site 4 out of 4 in the The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn502 b:21.4 occ:0.88 O D:HOH601 2.0 17.4 1.0 NE2 D:HIS58 2.1 20.0 1.0 NE2 D:HIS56 2.1 11.7 1.0 NE2 D:HIS232 2.1 21.2 1.0 OD1 D:ASP320 2.5 14.6 1.0 CD2 D:HIS58 3.0 17.7 1.0 CE1 D:HIS58 3.0 19.2 1.0 CE1 D:HIS232 3.0 16.3 1.0 CE1 D:HIS56 3.0 14.3 1.0 CD2 D:HIS56 3.2 14.3 1.0 CD2 D:HIS232 3.2 10.6 1.0 CG D:ASP320 3.3 20.8 1.0 OD2 D:ASP320 3.6 19.1 1.0 O D:HOH625 3.9 18.1 1.0 NE2 D:HIS269 4.1 15.7 1.0 ND1 D:HIS58 4.1 18.4 1.0 CG D:HIS58 4.1 21.0 1.0 N D:NFQ501 4.1 23.4 1.0 ND1 D:HIS232 4.2 17.0 1.0 ND1 D:HIS56 4.2 12.6 1.0 CG D:HIS232 4.3 11.0 1.0 CG D:HIS56 4.3 9.9 1.0 CF D:NFQ501 4.4 25.2 1.0 O1 D:NFQ501 4.4 19.9 1.0 CA D:NFQ501 4.4 25.2 1.0 NF D:NFQ501 4.4 17.8 1.0 C D:NFQ501 4.5 22.9 1.0 CB D:ASP320 4.6 16.0 1.0 CE1 D:HIS269 4.8 17.3 1.0 CG1 D:VAL268 4.9 10.2 1.0

A.A.Fedorov, E.V.Fedorov, R.Marti-Arbona, F.M.Raushel, S.C.Almo. The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Formimino-L-Aspartate To Be Published.