Zinc in PDB 4yhb: Crystal Structure of A Siderophore Utilization Protein From T. Fusca

The structure of Crystal Structure of A Siderophore Utilization Protein From T. Fusca, PDB code: 4yhb was solved by K.Li, S.D.Bruner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.74 / 1.89
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	129.541, 75.067, 73.904, 90.00, 102.62, 90.00
R / Rfree (%)	18.9 / 21.9

The binding sites of Zinc atom in the Crystal Structure of A Siderophore Utilization Protein From T. Fusca (pdb code 4yhb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of A Siderophore Utilization Protein From T. Fusca, PDB code: 4yhb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of A Siderophore Utilization Protein From T. Fusca


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A Siderophore Utilization Protein From T. Fusca within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:23.0 occ:0.85 NE2 A:HIS266 2.2 27.6 1.0 NE2 A:HIS265 2.2 21.4 1.0 NE2 A:HIS53 2.2 23.4 1.0 O A:HOH409 2.2 22.1 1.0 O A:HOH555 2.2 28.5 1.0 O A:HOH536 2.3 21.4 1.0 CE1 A:HIS53 3.0 22.7 1.0 CE1 A:HIS265 3.1 24.1 1.0 CE1 A:HIS266 3.1 25.7 1.0 CD2 A:HIS266 3.1 28.1 1.0 CD2 A:HIS265 3.2 20.1 1.0 CD2 A:HIS53 3.3 18.7 1.0 OD2 A:ASP88 4.1 28.3 1.0 ND1 A:HIS266 4.1 28.8 1.0 CG A:HIS266 4.2 27.5 1.0 ND1 A:HIS53 4.2 20.5 1.0 ND1 A:HIS265 4.2 21.6 1.0 O A:HOH597 4.3 33.8 1.0 CG A:HIS265 4.3 23.7 1.0 O A:HOH521 4.3 25.4 1.0 CG A:HIS53 4.3 20.2 1.0 O A:HOH579 4.4 33.8 1.0 O A:HOH508 4.6 28.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of A Siderophore Utilization Protein From T. Fusca


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of A Siderophore Utilization Protein From T. Fusca within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:28.6 occ:0.79 O B:HOH479 1.9 32.8 1.0 O B:HOH422 1.9 29.2 1.0 NE2 B:HIS53 2.1 28.7 1.0 O B:HOH506 2.3 36.0 1.0 NE2 B:HIS266 2.3 40.1 1.0 NE2 B:HIS265 2.3 30.2 1.0 CE1 B:HIS265 3.0 35.8 1.0 CE1 B:HIS53 3.0 26.6 1.0 CE1 B:HIS266 3.2 43.4 1.0 CD2 B:HIS53 3.2 25.6 1.0 CD2 B:HIS266 3.2 46.1 1.0 CD2 B:HIS265 3.3 36.6 1.0 OD2 B:ASP88 4.0 34.5 1.0 ND1 B:HIS265 4.1 42.4 1.0 O B:HOH498 4.2 40.3 1.0 ND1 B:HIS53 4.2 25.1 1.0 ND1 B:HIS266 4.3 43.1 1.0 O B:HOH515 4.3 28.4 1.0 CG B:HIS53 4.3 26.9 1.0 CG B:HIS265 4.3 35.4 1.0 CG B:HIS266 4.3 44.5 1.0 C3 B:MPD303 4.4 68.9 1.0 O B:HOH509 4.5 42.9 1.0 C5 B:MPD303 4.7 75.1 1.0 C7M B:FAD301 5.0 21.9 1.0 C4 B:MPD303 5.0 73.8 1.0

K.Li, W.H.Chen, S.D.Bruner. Structure and Mechanism of the Siderophore-Interacting Protein From the Fuscachelin Gene Cluster of Thermobifida Fusca. Biochemistry V. 54 3989 2015.
ISSN: ISSN 0006-2960
PubMed: 26043104
DOI: 10.1021/ACS.BIOCHEM.5B00354