Atomistry » Zinc » PDB 4r6t-4rlr » 4rdv
Atomistry »
  Zinc »
    PDB 4r6t-4rlr »
      4rdv »

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

Protein crystallography data

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

Zinc Binding Sites:

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 4rdv

Go back to Zinc Binding Sites List in 4rdv
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 4rdv

Go back to Zinc Binding Sites List in 4rdv
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 4rdv

Go back to Zinc Binding Sites List in 4rdv
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 4rdv

Go back to Zinc Binding Sites List in 4rdv
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

Reference:

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.
Page generated: Sun Oct 27 07:03:56 2024

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy