Zinc in PDB 1igb: Aeromonas Proteolytica Aminopeptidase Complexed with the Inhibitor Para-Iodo-D-Phenylalanine Hydroxamate

All present enzymatic activity of Aeromonas Proteolytica Aminopeptidase Complexed with the Inhibitor Para-Iodo-D-Phenylalanine Hydroxamate:
3.4.11.10;

The structure of Aeromonas Proteolytica Aminopeptidase Complexed with the Inhibitor Para-Iodo-D-Phenylalanine Hydroxamate, PDB code: 1igb was solved by B.Chevrier, H.D'orchymont, C.Schalk, C.Tarnus, D.Moras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.30
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	109.150, 109.150, 98.350, 90.00, 90.00, 120.00
R / Rfree (%)	16 / 24.1

The structure of Aeromonas Proteolytica Aminopeptidase Complexed with the Inhibitor Para-Iodo-D-Phenylalanine Hydroxamate also contains other interesting chemical elements:

Iodine

(I)

1 atom

The binding sites of Zinc atom in the Aeromonas Proteolytica Aminopeptidase Complexed with the Inhibitor Para-Iodo-D-Phenylalanine Hydroxamate (pdb code 1igb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Aeromonas Proteolytica Aminopeptidase Complexed with the Inhibitor Para-Iodo-D-Phenylalanine Hydroxamate, PDB code: 1igb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Aeromonas Proteolytica Aminopeptidase Complexed with the Inhibitor Para-Iodo-D-Phenylalanine Hydroxamate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aeromonas Proteolytica Aminopeptidase Complexed with the Inhibitor Para-Iodo-D-Phenylalanine Hydroxamate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:14.3 occ:1.00 HE2 A:HIS256 1.5 0.0 1.0 OE2 A:GLU152 2.0 4.8 1.0 OD2 A:ASP117 2.1 4.3 1.0 O3' A:IPO520 2.1 25.6 1.0 OE1 A:GLU152 2.3 3.0 1.0 O4' A:IPO520 2.4 4.5 1.0 NE2 A:HIS256 2.4 12.3 1.0 CD A:GLU152 2.5 9.6 1.0 C3' A:IPO520 3.0 20.2 1.0 CD2 A:HIS256 3.1 11.8 1.0 CG A:ASP117 3.1 11.0 1.0 N4' A:IPO520 3.1 21.8 1.0 H2 A:HOH743 3.3 0.0 1.0 H2 A:HOH604 3.4 0.0 1.0 OD1 A:ASP117 3.5 5.4 1.0 CE1 A:HIS256 3.5 14.5 1.0 ZN A:ZN502 3.6 14.7 1.0 CG A:GLU152 4.0 7.2 1.0 O A:HOH604 4.1 9.6 1.0 HE2 A:HIS97 4.2 0.0 1.0 OE1 A:GLU151 4.2 4.2 1.0 O A:HOH743 4.2 25.1 1.0 C2' A:IPO520 4.3 29.4 1.0 HN21 A:IPO520 4.3 0.0 1.0 CG A:HIS256 4.3 10.3 1.0 CB A:ASP117 4.5 4.7 1.0 ND1 A:HIS256 4.5 17.6 1.0 H2 A:HOH763 4.5 0.0 1.0 CD1 A:ILE255 4.6 2.4 1.0 H1 A:HOH763 4.7 0.0 1.0 O A:HOH763 4.7 31.8 1.0 C1' A:IPO520 4.7 30.0 1.0 H1 A:HOH604 4.7 0.0 1.0 NE2 A:HIS97 4.8 2.8 1.0 H1 A:HOH743 4.8 0.0 1.0 H1 A:HOH607 4.8 0.0 1.0 N2' A:IPO520 4.8 31.5 1.0 CE1 A:HIS97 4.8 4.0 1.0 CG2 A:THR101 4.9 2.5 1.0 CB A:GLU152 5.0 7.3 1.0

Zinc binding site 2 out of 2 in the Aeromonas Proteolytica Aminopeptidase Complexed with the Inhibitor Para-Iodo-D-Phenylalanine Hydroxamate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Aeromonas Proteolytica Aminopeptidase Complexed with the Inhibitor Para-Iodo-D-Phenylalanine Hydroxamate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:14.7 occ:1.00 HE2 A:HIS97 1.2 0.0 1.0 O4' A:IPO520 1.8 4.5 1.0 OD1 A:ASP117 1.9 5.4 1.0 OD1 A:ASP179 2.0 11.5 1.0 NE2 A:HIS97 2.2 2.8 1.0 OD2 A:ASP179 2.5 13.1 1.0 CG A:ASP179 2.6 10.5 1.0 N4' A:IPO520 2.8 21.8 1.0 CG A:ASP117 3.0 11.0 1.0 CD2 A:HIS97 3.1 9.0 1.0 CE1 A:HIS97 3.1 4.0 1.0 OD2 A:ASP117 3.3 4.3 1.0 ZN A:ZN501 3.6 14.3 1.0 OE1 A:GLU151 3.8 4.2 1.0 C3' A:IPO520 3.9 20.2 1.0 OE2 A:GLU152 3.9 4.8 1.0 CB A:ASP179 4.1 2.1 1.0 ND1 A:HIS97 4.2 9.0 1.0 CD A:GLU151 4.2 2.6 1.0 CG A:HIS97 4.2 4.7 1.0 CB A:ASP117 4.3 4.7 1.0 CB A:ASP118 4.4 2.5 1.0 O3' A:IPO520 4.4 25.6 1.0 OE2 A:GLU151 4.4 10.9 1.0 CD A:GLU152 4.6 9.6 1.0 CA A:ASP117 4.6 8.6 1.0 H2 A:HOH604 4.7 0.0 1.0 HG A:SER228 4.7 0.0 1.0 H A:ASP118 4.8 0.0 1.0 N A:ASP118 4.8 8.1 1.0 CA A:ASP179 4.8 6.6 1.0 CG A:MET180 4.9 2.0 1.0 SD A:MET180 4.9 4.8 1.0 OG A:SER228 4.9 4.5 1.0 OE1 A:GLU152 4.9 3.0 1.0 C A:ASP117 4.9 4.7 1.0 CG A:ASP118 5.0 2.9 1.0

B.Chevrier, H.D'orchymont, C.Schalk, C.Tarnus, D.Moras. The Structure of the Aeromonas Proteolytica Aminopeptidase Complexed with A Hydroxamate Inhibitor. Involvement in Catalysis of GLU151 and Two Zinc Ions of the Co-Catalytic Unit. Eur.J.Biochem. V. 237 393 1996.
ISSN: ISSN 0014-2956
PubMed: 8647077
DOI: 10.1111/J.1432-1033.1996.0393K.X