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Zinc in PDB 3mdu: The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Guanidino-L-Glutamate

Protein crystallography data

The structure of The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Guanidino-L-Glutamate, PDB code: 3mdu 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) 35.43 / 1.40
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 133.208, 133.208, 124.835, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 18.9

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-Guanidino-L-Glutamate (pdb code 3mdu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Guanidino-L-Glutamate, PDB code: 3mdu:

Zinc binding site 1 out of 1 in 3mdu

Go back to Zinc Binding Sites List in 3mdu
Zinc binding site 1 out of 1 in the The Structure of N-Formimino-L-Glutamate Iminohydrolase From Pseudomonas Aeruginosa Complexed with N-Guanidino-L-Glutamate


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-Guanidino-L-Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn454

b:18.0
occ:1.00
O A:HOH495 1.9 20.7 1.0
NE2 A:HIS58 2.1 17.1 1.0
NE2 A:HIS56 2.1 17.1 1.0
NE2 A:HIS232 2.1 18.7 1.0
OD1 A:ASP320 2.5 17.7 1.0
CE1 A:HIS58 3.0 16.5 1.0
CE1 A:HIS56 3.0 14.8 1.0
CD2 A:HIS58 3.1 16.8 1.0
CD2 A:HIS232 3.1 20.1 1.0
CD2 A:HIS56 3.1 16.5 1.0
CE1 A:HIS232 3.2 18.8 1.0
CG A:ASP320 3.4 18.0 1.0
OD2 A:ASP320 3.6 17.9 1.0
N A:NGQ455 3.8 25.1 1.0
O A:HOH499 4.0 20.8 1.0
NE2 A:HIS269 4.1 21.2 1.0
ND1 A:HIS58 4.1 16.4 1.0
ND1 A:HIS56 4.1 16.2 1.0
CG A:HIS58 4.2 15.6 1.0
CF A:NGQ455 4.2 25.1 1.0
CG A:HIS56 4.2 14.9 1.0
ND1 A:HIS232 4.2 19.7 1.0
CG A:HIS232 4.3 19.4 1.0
O1 A:NGQ455 4.4 23.4 1.0
C A:NGQ455 4.5 23.4 1.0
NG A:NGQ455 4.5 24.4 1.0
CA A:NGQ455 4.5 22.9 1.0
CB A:ASP320 4.7 16.1 1.0
CE1 A:HIS269 4.7 19.4 1.0
NF A:NGQ455 4.7 25.4 1.0
CG1 A:VAL268 4.9 16.6 1.0

Reference:

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
Page generated: Wed Dec 16 04:34:51 2020

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