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Calcium in PDB 3nqz: Crystal Structure of the Autoprocessed Vibriolysin Mcp-02 with E369A Mutation

Enzymatic activity of Crystal Structure of the Autoprocessed Vibriolysin Mcp-02 with E369A Mutation

All present enzymatic activity of Crystal Structure of the Autoprocessed Vibriolysin Mcp-02 with E369A Mutation:
3.4.24.25;

Protein crystallography data

The structure of Crystal Structure of the Autoprocessed Vibriolysin Mcp-02 with E369A Mutation, PDB code: 3nqz was solved by X.Gao, J.Wang, L.Chen, J.-W.Wu, Y.-Z.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 16.97 / 2.05
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 82.535, 82.535, 154.206, 90.00, 90.00, 120.00
R / Rfree (%) 17.9 / 22

Other elements in 3nqz:

The structure of Crystal Structure of the Autoprocessed Vibriolysin Mcp-02 with E369A Mutation also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Autoprocessed Vibriolysin Mcp-02 with E369A Mutation (pdb code 3nqz). 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 the Autoprocessed Vibriolysin Mcp-02 with E369A Mutation, PDB code: 3nqz:

Calcium binding site 1 out of 1 in 3nqz

Go back to Calcium Binding Sites List in 3nqz
Calcium binding site 1 out of 1 in the Crystal Structure of the Autoprocessed Vibriolysin Mcp-02 with E369A Mutation


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 the Autoprocessed Vibriolysin Mcp-02 with E369A Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca520

b:19.2
occ:1.00
 O B:LEU390 2.4 18.5 1.0
OE2 B:GLU380 2.5 13.9 1.0
OE2 B:GLU377 2.5 15.1 1.0
OD1 B:ASP388 2.5 16.2 1.0
O B:HOH638 2.5 20.9 1.0
OD2 B:ASP341 2.6 10.9 1.0
OE1 B:GLU380 2.7 12.2 1.0
CD B:GLU380 2.9 13.1 1.0
CD B:GLU377 3.4 13.9 1.0
C B:LEU390 3.5 16.1 1.0
CG B:ASP341 3.6 9.8 1.0
CG B:ASP388 3.6 14.7 1.0
OE1 B:GLU377 3.6 15.8 1.0
OD2 B:ASP388 3.9 16.9 1.0
N B:LEU390 4.0 14.2 1.0
CB B:ASP341 4.0 10.5 1.0
O B:HOH637 4.3 15.6 1.0
CA B:LEU390 4.3 16.1 1.0
CG B:GLU380 4.4 12.8 1.0
N B:VAL391 4.4 13.5 1.0
CA B:VAL391 4.4 12.0 1.0
O B:HOH28 4.5 9.0 1.0
OD1 B:ASP341 4.5 10.5 1.0
N B:TRP389 4.6 12.6 1.0
N B:GLY392 4.6 11.3 1.0
N B:ASP388 4.7 13.2 1.0
O B:HOH66 4.7 12.2 1.0
CG B:GLU377 4.8 8.7 1.0
CB B:LEU390 4.8 16.4 1.0
C B:TRP389 4.9 14.2 1.0
CB B:ASP388 4.9 13.9 1.0
C B:VAL391 5.0 11.1 1.0

Reference:

X.Gao, J.Wang, D.-Q.Yu, F.Bian, B.-B.Xie, X.-L.Chen, B.-C.Zhou, L.-H.Lai, Z.-X.Wang, J.-W.Wu, Y.-Z.Zhang. Structural Basis For the Autoprocessing of Zinc Metalloproteases in the Thermolysin Family Proc.Natl.Acad.Sci.Usa V. 107 17569 2010.
ISSN: ISSN 0027-8424
PubMed: 20876133
DOI: 10.1073/PNAS.1005681107
Page generated: Sat Jul 13 15:07:58 2024

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