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Chlorine in PDB 3ng3: Crystal Structure of Deoxyribose Phosphate Aldolase From Mycobacterium Avium 104 in A Schiff Base with An Unknown Aldehyde

Enzymatic activity of Crystal Structure of Deoxyribose Phosphate Aldolase From Mycobacterium Avium 104 in A Schiff Base with An Unknown Aldehyde

All present enzymatic activity of Crystal Structure of Deoxyribose Phosphate Aldolase From Mycobacterium Avium 104 in A Schiff Base with An Unknown Aldehyde:
4.1.2.4;

Protein crystallography data

The structure of Crystal Structure of Deoxyribose Phosphate Aldolase From Mycobacterium Avium 104 in A Schiff Base with An Unknown Aldehyde, PDB code: 3ng3 was solved by Ssgcid, 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) 44.78 / 2.15
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.480, 116.320, 101.280, 90.00, 105.76, 90.00
R / Rfree (%) 18.6 / 22.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Deoxyribose Phosphate Aldolase From Mycobacterium Avium 104 in A Schiff Base with An Unknown Aldehyde (pdb code 3ng3). 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 Deoxyribose Phosphate Aldolase From Mycobacterium Avium 104 in A Schiff Base with An Unknown Aldehyde, PDB code: 3ng3:

Chlorine binding site 1 out of 1 in 3ng3

Go back to Chlorine Binding Sites List in 3ng3
Chlorine binding site 1 out of 1 in the Crystal Structure of Deoxyribose Phosphate Aldolase From Mycobacterium Avium 104 in A Schiff Base with An Unknown Aldehyde


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 Deoxyribose Phosphate Aldolase From Mycobacterium Avium 104 in A Schiff Base with An Unknown Aldehyde within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl224

b:24.0
occ:1.00
OG1 A:THR195 3.1 24.1 1.0
O A:HOH291 3.2 8.0 1.0
CG2 A:THR195 3.8 22.9 1.0
CB A:ALA197 3.8 20.8 1.0
CB A:THR195 3.8 23.8 1.0
OD1 A:ASP198 4.5 24.0 1.0
O A:HOH270 4.6 8.3 1.0
N A:ASP198 4.7 20.1 1.0
CA A:ALA197 4.9 20.9 1.0
CG A:ASP198 4.9 21.9 1.0

Reference:

L.Baugh, I.Phan, D.W.Begley, M.C.Clifton, B.Armour, D.M.Dranow, B.M.Taylor, M.M.Muruthi, J.Abendroth, J.W.Fairman, D.Fox, S.H.Dieterich, B.L.Staker, A.S.Gardberg, R.Choi, S.N.Hewitt, A.J.Napuli, J.Myers, L.K.Barrett, Y.Zhang, M.Ferrell, E.Mundt, K.Thompkins, N.Tran, S.Lyons-Abbott, A.Abramov, A.Sekar, D.Serbzhinskiy, D.Lorimer, G.W.Buchko, R.Stacy, L.J.Stewart, T.E.Edwards, W.C.Van Voorhis, P.J.Myler. Increasing the Structural Coverage of Tuberculosis Drug Targets. Tuberculosis (Edinb) V. 95 142 2015.
ISSN: ISSN 1472-9792
PubMed: 25613812
DOI: 10.1016/J.TUBE.2014.12.003
Page generated: Sat Dec 12 09:57:36 2020

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