Iron in PDB 3ojg: Structure of An Inactive Lactonase From Geobacillus Kaustophilus with Bound N-Butyryl-Dl-Homoserine Lactone

The structure of Structure of An Inactive Lactonase From Geobacillus Kaustophilus with Bound N-Butyryl-Dl-Homoserine Lactone, PDB code: 3ojg was solved by B.Xue, J.Y.Chow, A.Tung, R.C.Robinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.12 / 1.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	70.269, 76.244, 134.408, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 21.9

The structure of Structure of An Inactive Lactonase From Geobacillus Kaustophilus with Bound N-Butyryl-Dl-Homoserine Lactone also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Iron atom in the Structure of An Inactive Lactonase From Geobacillus Kaustophilus with Bound N-Butyryl-Dl-Homoserine Lactone (pdb code 3ojg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Structure of An Inactive Lactonase From Geobacillus Kaustophilus with Bound N-Butyryl-Dl-Homoserine Lactone, PDB code: 3ojg:

Iron binding site 1 out of 1 in the Structure of An Inactive Lactonase From Geobacillus Kaustophilus with Bound N-Butyryl-Dl-Homoserine Lactone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of An Inactive Lactonase From Geobacillus Kaustophilus with Bound N-Butyryl-Dl-Homoserine Lactone within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:18.9 occ:0.43 OQ1 A:KCX145 2.2 31.6 1.0 NE2 A:HIS206 2.2 27.2 1.0 ND1 A:HIS178 2.2 17.3 1.0 O A:HOH466 2.6 57.5 1.0 CD2 A:HIS206 3.1 22.4 1.0 CE1 A:HIS178 3.2 17.7 1.0 CX A:KCX145 3.2 33.7 1.0 CE1 A:HIS206 3.2 24.1 1.0 CG A:HIS178 3.3 15.9 1.0 ZN A:ZN401 3.5 19.5 0.4 OQ2 A:KCX145 3.6 28.6 1.0 CB A:HIS178 3.6 15.7 1.0 NH2 A:ARG230 3.6 34.8 1.0 OH A:TYR99 3.9 25.9 1.0 CE1 A:TYR99 3.9 22.3 1.0 CG A:HIS206 4.3 17.1 1.0 NE2 A:HIS178 4.3 17.0 1.0 ND1 A:HIS206 4.3 18.8 1.0 CD2 A:HIS178 4.4 18.1 1.0 CE1 A:HIS23 4.4 28.1 1.0 CZ A:TYR99 4.4 24.0 1.0 NZ A:KCX145 4.4 30.6 1.0 CA A:HIS178 4.4 15.9 1.0 CZ A:ARG230 4.5 34.3 1.0 NE2 A:HIS23 4.5 27.8 1.0 ND2 A:ASN266 4.5 32.2 1.0 NE A:ARG230 4.8 30.8 1.0 CE A:KCX145 4.8 27.9 1.0 OD1 A:ASN266 4.8 22.3 1.0 O6 A:HL4327 4.9 59.7 0.9 OAP A:HL4327 5.0 56.6 0.9

J.Y.Chow, B.Xue, K.H.Lee, A.Tung, L.Wu, R.C.Robinson, W.S.Yew. Directed Evolution of A Thermostable Quorum-Quenching Lactonase From the Amidohydrolase Superfamily J.Biol.Chem. V. 285 40911 2010.
ISSN: ISSN 0021-9258
PubMed: 20980257
DOI: 10.1074/JBC.M110.177139