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Chlorine in PDB 3uqa: Crystal Structure of A Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation A54E From Burkholderia Pseudomallei Complexed with FK506

Enzymatic activity of Crystal Structure of A Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation A54E From Burkholderia Pseudomallei Complexed with FK506

All present enzymatic activity of Crystal Structure of A Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation A54E From Burkholderia Pseudomallei Complexed with FK506:
5.2.1.8;

Protein crystallography data

The structure of Crystal Structure of A Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation A54E From Burkholderia Pseudomallei Complexed with FK506, PDB code: 3uqa was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.72 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 96.310, 31.280, 74.320, 90.00, 121.57, 90.00
R / Rfree (%) 18.2 / 19.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation A54E From Burkholderia Pseudomallei Complexed with FK506 (pdb code 3uqa). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of A Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation A54E From Burkholderia Pseudomallei Complexed with FK506, PDB code: 3uqa:

Chlorine binding site 1 out of 1 in 3uqa

Go back to Chlorine Binding Sites List in 3uqa
Chlorine binding site 1 out of 1 in the Crystal Structure of A Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation A54E From Burkholderia Pseudomallei Complexed with FK506


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of A Smt Fusion Peptidyl-Prolyl Cis-Trans Isomerase with Surface Mutation A54E From Burkholderia Pseudomallei Complexed with FK506 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl116

b:22.0
occ:1.00
 O A:HOH120 3.0 32.3 1.0
O A:HOH143 3.1 33.2 1.0
NE A:ARG-52 3.3 25.5 1.0
CA A:ASP-23 3.7 20.1 1.0
O A:ALA-24 3.8 18.8 1.0
CB A:PRO-54 3.8 21.7 1.0
CD A:ARG-52 3.8 25.3 1.0
CB A:ASP-23 3.9 22.0 1.0
CB A:ARG-52 4.0 20.9 1.0
N A:ASP-23 4.1 18.6 1.0
C A:ALA-24 4.1 18.6 1.0
CG A:PRO-54 4.1 24.0 1.0
CZ A:ARG-52 4.4 28.9 1.0
NH2 A:ARG-52 4.5 29.1 1.0
CG A:ARG-52 4.6 22.4 1.0
C A:ASP-23 4.8 19.6 1.0
CB A:ALA-24 4.9 18.2 1.0

Reference:

D.W.Begley, D.Fox, D.Jenner, C.Juli, P.G.Pierce, J.Abendroth, M.Muruthi, K.Safford, V.Anderson, K.Atkins, S.R.Barnes, S.O.Moen, A.C.Raymond, R.Stacy, P.J.Myler, B.L.Staker, N.J.Harmer, I.H.Norville, U.Holzgrabe, M.Sarkar-Tyson, T.E.Edwards, D.D.Lorimer. A Structural Biology Approach Enables the Development of Antimicrobials Targeting Bacterial Immunophilins. Antimicrob.Agents Chemother. V. 58 1458 2014.
ISSN: ISSN 0066-4804
PubMed: 24366729
DOI: 10.1128/AAC.01875-13
Page generated: Sun Jul 21 06:24:35 2024

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