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

Protein crystallography data

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

Other elements in 3ojg:

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

Iron (Fe) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Structure of An Inactive Lactonase From Geobacillus Kaustophilus with Bound N-Butyryl-Dl-Homoserine Lactone, PDB code: 3ojg:

Zinc binding site 1 out of 1 in 3ojg

Go back to Zinc Binding Sites List in 3ojg
Zinc 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 Zinc with other atoms in the Zn 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:Zn401

b:19.5
occ:0.38
NE2 A:HIS25 2.1 22.8 1.0
OD1 A:ASN266 2.1 22.3 1.0
NE2 A:HIS23 2.3 27.8 1.0
OQ2 A:KCX145 2.4 28.6 1.0
O A:HOH466 2.9 57.5 1.0
CE1 A:HIS25 3.0 20.7 1.0
CG A:ASN266 3.1 28.4 1.0
CD2 A:HIS23 3.1 28.3 1.0
CD2 A:HIS25 3.2 19.9 1.0
CX A:KCX145 3.2 33.7 1.0
CE1 A:HIS23 3.3 28.1 1.0
OQ1 A:KCX145 3.3 31.6 1.0
ND2 A:ASN266 3.5 32.2 1.0
FE A:FE402 3.5 18.9 0.4
ND1 A:HIS25 4.1 19.7 1.0
OAP A:HL4327 4.2 56.6 0.9
CG A:HIS25 4.2 17.5 1.0
CG A:HIS23 4.3 26.8 1.0
NZ A:KCX145 4.3 30.6 1.0
ND1 A:HIS23 4.3 29.6 1.0
CE1 A:HIS206 4.3 24.1 1.0
NE2 A:HIS206 4.4 27.2 1.0
CB A:ASN266 4.5 19.1 1.0
CA A:ASN266 4.9 17.2 1.0

Reference:

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
Page generated: Wed Dec 16 04:40:36 2020

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