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Calcium in PDB 5bmw: Crystal Structure of T75V Mutant of Triosephosphate Isomerase From Plasmodium Falciparum

Enzymatic activity of Crystal Structure of T75V Mutant of Triosephosphate Isomerase From Plasmodium Falciparum

All present enzymatic activity of Crystal Structure of T75V Mutant of Triosephosphate Isomerase From Plasmodium Falciparum:
5.3.1.1;

Protein crystallography data

The structure of Crystal Structure of T75V Mutant of Triosephosphate Isomerase From Plasmodium Falciparum, PDB code: 5bmw was solved by D.Bandyopadhyay, M.R.N.Murthy, H.Balaram, P.Balaram, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 73.73 / 1.86
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.210, 76.020, 74.360, 90.00, 97.47, 90.00
R / Rfree (%) 13.1 / 18.2

Other elements in 5bmw:

The structure of Crystal Structure of T75V Mutant of Triosephosphate Isomerase From Plasmodium Falciparum also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of T75V Mutant of Triosephosphate Isomerase From Plasmodium Falciparum (pdb code 5bmw). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of T75V Mutant of Triosephosphate Isomerase From Plasmodium Falciparum, PDB code: 5bmw:

Calcium binding site 1 out of 1 in 5bmw

Go back to Calcium Binding Sites List in 5bmw
Calcium binding site 1 out of 1 in the Crystal Structure of T75V Mutant of Triosephosphate Isomerase From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of T75V Mutant of Triosephosphate Isomerase From Plasmodium Falciparum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca309

b:10.8
occ:1.00
 O A:MET248 2.4 10.0 1.0
O2 A:EDO305 2.4 9.4 1.0
O A:HOH511 2.4 12.3 1.0
O1 A:EDO305 2.5 9.6 1.0
C1 A:EDO305 3.3 9.5 1.0
C2 A:EDO305 3.3 9.1 1.0
C A:MET248 3.6 10.6 1.0
O A:HOH426 4.1 15.8 1.0
OXT A:MET248 4.2 10.3 1.0
O A:SER246 4.3 7.7 1.0
NE2 A:GLN222 4.4 8.8 1.0
N A:MET248 4.5 8.9 1.0
CA A:MET248 4.7 9.7 1.0
O A:HOH457 4.7 22.8 1.0
C A:ALA247 4.8 8.7 1.0

Reference:

D.Bandyopadhyay, M.R.Murthy, H.Balaram, P.Balaram. Probing the Role of Highly Conserved Residues in Triosephosphate Isomerase - Analysis of Site Specific Mutants at Positions 64 and 75 in the Plasmodial Enzyme Febs J. V. 282 3863 2015.
ISSN: ISSN 1742-464X
PubMed: 26206206
DOI: 10.1111/FEBS.13384
Page generated: Sun Jul 14 16:54:04 2024

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