Zinc in PDB 3qdh: Crystal Structure of Actinomyces Fimbrial Adhesin Fima

The structure of Crystal Structure of Actinomyces Fimbrial Adhesin Fima, PDB code: 3qdh was solved by B.Devarajan, V.Krishnan, S.V.L.Narayana, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.528, 39.799, 77.139, 90.00, 98.34, 90.00
R / Rfree (%)	20.9 / 24.9

The binding sites of Zinc atom in the Crystal Structure of Actinomyces Fimbrial Adhesin Fima (pdb code 3qdh). 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 Crystal Structure of Actinomyces Fimbrial Adhesin Fima, PDB code: 3qdh:

Zinc binding site 1 out of 1 in the Crystal Structure of Actinomyces Fimbrial Adhesin Fima


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 Actinomyces Fimbrial Adhesin Fima within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:15.4 occ:1.00 OE1 A:GLU288 2.0 17.9 1.0 OD2 A:ASP268 2.0 16.2 1.0 OD1 A:ASP271 2.0 13.4 1.0 CG A:ASP268 2.8 15.4 1.0 CG A:ASP271 2.9 14.3 1.0 OD1 A:ASP268 2.9 16.3 1.0 CD A:GLU288 3.1 20.1 1.0 OD2 A:ASP271 3.2 13.9 1.0 CB A:GLU288 3.5 13.6 1.0 CG A:GLU288 3.6 17.9 1.0 NH2 A:ARG292 3.8 14.4 1.0 OG1 A:THR270 3.9 17.2 1.0 NE A:ARG292 4.0 16.7 1.0 OE2 A:GLU288 4.2 25.8 1.0 CB A:ASP271 4.2 13.7 1.0 CB A:ASP268 4.2 16.4 1.0 CZ A:ARG292 4.3 17.1 1.0 N A:ASP271 4.4 14.3 1.0 CA A:ASP271 4.4 14.1 1.0 C A:THR270 4.6 15.6 1.0 O A:THR270 4.8 15.5 1.0 CA A:GLU288 4.8 12.8 1.0 N A:ASP268 4.8 16.0 1.0 C A:GLU288 4.9 11.9 1.0

A.Mishra, B.Devarajan, M.E.Reardon, P.Dwivedi, V.Krishnan, J.O.Cisar, A.Das, S.V.Narayana, H.Ton-That. Two Autonomous Structural Modules in the Fimbrial Shaft Adhesin Fima Mediate Actinomyces Interactions with Streptococci and Host Cells During Oral Biofilm Development. Mol.Microbiol. V. 81 1205 2011.
ISSN: ISSN 0950-382X
PubMed: 21696465
DOI: 10.1111/J.1365-2958.2011.07745.X