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Chlorine in PDB 4dxl: Crystal Structure of Ispe (4-Diphosphocytidyl-2-C-Methyl-D-Erythritol Kinase) From Mycobacterium Abscessus, Bound to Cmp and Atp

Enzymatic activity of Crystal Structure of Ispe (4-Diphosphocytidyl-2-C-Methyl-D-Erythritol Kinase) From Mycobacterium Abscessus, Bound to Cmp and Atp

All present enzymatic activity of Crystal Structure of Ispe (4-Diphosphocytidyl-2-C-Methyl-D-Erythritol Kinase) From Mycobacterium Abscessus, Bound to Cmp and Atp:
2.7.1.148;

Protein crystallography data

The structure of Crystal Structure of Ispe (4-Diphosphocytidyl-2-C-Methyl-D-Erythritol Kinase) From Mycobacterium Abscessus, Bound to Cmp and Atp, PDB code: 4dxl 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) 35.56 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 46.590, 110.090, 53.290, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 25.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Ispe (4-Diphosphocytidyl-2-C-Methyl-D-Erythritol Kinase) From Mycobacterium Abscessus, Bound to Cmp and Atp (pdb code 4dxl). 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 Ispe (4-Diphosphocytidyl-2-C-Methyl-D-Erythritol Kinase) From Mycobacterium Abscessus, Bound to Cmp and Atp, PDB code: 4dxl:

Chlorine binding site 1 out of 1 in 4dxl

Go back to Chlorine Binding Sites List in 4dxl
Chlorine binding site 1 out of 1 in the Crystal Structure of Ispe (4-Diphosphocytidyl-2-C-Methyl-D-Erythritol Kinase) From Mycobacterium Abscessus, Bound to Cmp and Atp


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 Ispe (4-Diphosphocytidyl-2-C-Methyl-D-Erythritol Kinase) From Mycobacterium Abscessus, Bound to Cmp and Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:47.0
occ:1.00
 O A:HOH550 3.2 11.5 1.0
O A:HOH706 3.4 33.6 1.0
ND1 A:HIS154 3.7 9.1 1.0
CB A:HIS154 4.1 8.3 1.0
CA A:HIS154 4.1 8.1 1.0
CG A:HIS154 4.2 8.5 1.0
N A:HIS154 4.5 7.9 1.0
ND1 A:HIS139 4.6 12.5 1.0
CE1 A:HIS154 4.7 9.1 1.0
CB A:LEU153 4.8 8.2 1.0
CB A:HIS139 4.8 13.1 1.0
C A:LEU153 4.8 8.0 1.0
O A:LEU153 4.9 8.4 1.0
O A:ARG135 4.9 15.2 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: Sun Jul 21 12:22:06 2024

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