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Calcium in PDB 4m8u: The Structure of Mall Mutant Enzyme V200A From Bacillus Subtilus

Enzymatic activity of The Structure of Mall Mutant Enzyme V200A From Bacillus Subtilus

All present enzymatic activity of The Structure of Mall Mutant Enzyme V200A From Bacillus Subtilus:
3.2.1.10;

Protein crystallography data

The structure of The Structure of Mall Mutant Enzyme V200A From Bacillus Subtilus, PDB code: 4m8u was solved by J.K.Hobbs, W.Jiao, A.D.Easter, E.J.Parker, L.A.Schipper, V.L.Arcus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.28 / 1.45
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.650, 100.330, 61.360, 90.00, 112.59, 90.00
R / Rfree (%) 13.8 / 16.4

Calcium Binding Sites:

The binding sites of Calcium atom in the The Structure of Mall Mutant Enzyme V200A From Bacillus Subtilus (pdb code 4m8u). 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 The Structure of Mall Mutant Enzyme V200A From Bacillus Subtilus, PDB code: 4m8u:

Calcium binding site 1 out of 1 in 4m8u

Go back to Calcium Binding Sites List in 4m8u
Calcium binding site 1 out of 1 in the The Structure of Mall Mutant Enzyme V200A From Bacillus Subtilus


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Structure of Mall Mutant Enzyme V200A From Bacillus Subtilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca603

b:10.2
occ:1.00
OD1 A:ASN22 2.2 14.9 1.0
O A:PHE26 2.2 10.0 1.0
OD2 A:ASP28 2.3 12.4 1.0
OD1 A:ASP20 2.3 12.1 1.0
O A:HOH701 2.3 12.8 1.0
OD1 A:ASP24 2.4 13.3 1.0
CG A:ASP24 3.3 14.1 1.0
CG A:ASN22 3.3 16.7 1.0
CG A:ASP28 3.3 11.6 1.0
CG A:ASP20 3.4 12.0 1.0
C A:PHE26 3.5 10.1 1.0
OD2 A:ASP24 3.7 15.4 1.0
CB A:ASP28 3.8 11.0 1.0
ND2 A:ASN22 3.9 20.1 1.0
N A:PHE26 4.1 11.4 1.0
N A:ASN22 4.1 14.1 1.0
OD2 A:ASP20 4.2 13.1 1.0
CA A:PHE26 4.2 10.4 1.0
N A:ASP24 4.2 14.6 1.0
CB A:ASP20 4.3 11.3 1.0
CA A:ASP20 4.3 11.1 1.0
CB A:PHE26 4.4 10.8 1.0
OD1 A:ASP28 4.4 12.3 1.0
CB A:ASN22 4.4 16.3 1.0
N A:GLY23 4.4 15.1 1.0
CB A:ASP24 4.4 14.7 1.0
O A:LYS73 4.4 13.0 1.0
C A:GLY27 4.5 9.6 1.0
CA A:ASN22 4.5 15.5 1.0
N A:ASP28 4.5 9.7 1.0
N A:GLY27 4.6 9.1 1.0
N A:ALA21 4.6 12.4 1.0
C A:ASP20 4.6 11.9 1.0
C A:ASN22 4.6 15.8 1.0
CA A:GLY27 4.7 9.4 1.0
CA A:ASP24 4.7 14.8 1.0
CA A:ASP28 4.8 10.0 1.0
O A:GLY27 4.8 9.5 1.0
N A:GLY25 4.8 13.5 1.0

Reference:

J.K.Hobbs, W.Jiao, A.D.Easter, E.J.Parker, L.A.Schipper, V.L.Arcus. Change in Heat Capacity For Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates. Acs Chem.Biol. V. 8 2388 2013.
ISSN: ISSN 1554-8929
PubMed: 24015933
DOI: 10.1021/CB4005029
Page generated: Wed Jul 9 00:19:05 2025

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