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Cobalt in PDB 4hcq: Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Glucosamine-1-Phosphate

Enzymatic activity of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Glucosamine-1-Phosphate

All present enzymatic activity of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Glucosamine-1-Phosphate:
2.3.1.157; 2.7.7.23;

Protein crystallography data

The structure of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Glucosamine-1-Phosphate, PDB code: 4hcq was solved by P.K.A.Jagtap, S.K.Verma, N.Vithani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.93 / 2.60
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 79.270, 79.270, 276.730, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 26.5

Other elements in 4hcq:

The structure of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Glucosamine-1-Phosphate also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Glucosamine-1-Phosphate (pdb code 4hcq). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Glucosamine-1-Phosphate, PDB code: 4hcq:

Cobalt binding site 1 out of 1 in 4hcq

Go back to Cobalt Binding Sites List in 4hcq
Cobalt binding site 1 out of 1 in the Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Glucosamine-1-Phosphate


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Glucosamine-1-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co503

b:37.3
occ:0.33
OD2 A:ASP417 1.7 32.9 1.0
CG A:ASP417 2.4 26.1 1.0
OD1 A:ASP417 2.4 29.8 1.0
MG A:MG504 3.5 28.9 0.3
O A:HOH614 3.6 25.8 1.0
CB A:ASP417 3.9 21.8 1.0
O A:ASP417 4.5 19.8 1.0
CA A:GLY435 4.7 21.0 1.0
CA A:ASP417 4.9 21.4 1.0
O A:HOH687 4.9 28.6 1.0

Reference:

P.K.A.Jagtap, S.K.Verma, N.Vithani, V.S.Bais, B.Prakash. Crystal Structures Identify An Atypical Two-Metal-Ion Mechanism For Uridyltransfer in Glmu: Its Significance to Sugar Nucleotidyl Transferases J.Mol.Biol. V. 425 1745 2013.
ISSN: ISSN 0022-2836
PubMed: 23485416
DOI: 10.1016/J.JMB.2013.02.019
Page generated: Tue Jul 30 17:09:33 2024

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