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Zinc in PDB 3nqy: Crystal Structure of the Autoprocessed Complex of Vibriolysin Mcp-02 with A Single Point Mutation E346A

Enzymatic activity of Crystal Structure of the Autoprocessed Complex of Vibriolysin Mcp-02 with A Single Point Mutation E346A

All present enzymatic activity of Crystal Structure of the Autoprocessed Complex of Vibriolysin Mcp-02 with A Single Point Mutation E346A:
3.4.24.25;

Protein crystallography data

The structure of Crystal Structure of the Autoprocessed Complex of Vibriolysin Mcp-02 with A Single Point Mutation E346A, PDB code: 3nqy was solved by X.Gao, J.Wang, 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) 23.68 / 2.60
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 83.009, 83.009, 154.216, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 25

Other elements in 3nqy:

The structure of Crystal Structure of the Autoprocessed Complex of Vibriolysin Mcp-02 with A Single Point Mutation E346A also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Autoprocessed Complex of Vibriolysin Mcp-02 with A Single Point Mutation E346A (pdb code 3nqy). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Autoprocessed Complex of Vibriolysin Mcp-02 with A Single Point Mutation E346A, PDB code: 3nqy:

Zinc binding site 1 out of 1 in 3nqy

Go back to Zinc Binding Sites List in 3nqy
Zinc binding site 1 out of 1 in the Crystal Structure of the Autoprocessed Complex of Vibriolysin Mcp-02 with A Single Point Mutation E346A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Autoprocessed Complex of Vibriolysin Mcp-02 with A Single Point Mutation E346A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn520

b:30.0
occ:1.00
 OXT A:HIS204 1.9 30.0 1.0
NE2 B:HIS345 2.0 24.9 1.0
NE2 B:HIS349 2.0 24.2 1.0
OE1 B:GLU369 2.2 25.9 1.0
CD2 B:HIS349 2.9 19.8 1.0
CE1 B:HIS345 3.0 21.8 1.0
CD2 B:HIS345 3.0 21.8 1.0
C A:HIS204 3.0 20.0 1.0
CD B:GLU369 3.0 25.6 1.0
CE1 B:HIS349 3.0 22.9 1.0
OE2 B:GLU369 3.2 19.0 1.0
O A:HIS204 3.3 20.0 1.0
OH B:TYR360 3.9 23.6 1.0
ND1 B:HIS345 4.0 24.1 1.0
CG B:HIS349 4.1 22.8 1.0
CG B:HIS345 4.1 25.2 1.0
ND1 B:HIS349 4.1 20.3 1.0
NE2 B:HIS428 4.3 24.9 1.0
CA A:HIS204 4.3 20.0 1.0
CB B:SER372 4.4 20.1 1.0
CG B:GLU369 4.4 22.6 1.0
C A:GLN203 4.5 24.7 1.0
OG B:SER372 4.6 22.2 1.0
N A:HIS204 4.6 20.0 1.0
O A:GLN203 4.7 24.5 1.0
CD2 B:HIS428 4.8 23.8 1.0
CE1 B:TYR360 4.8 23.3 1.0
CZ B:TYR360 4.8 23.5 1.0
CA B:GLU369 4.8 21.9 1.0
O B:HIS345 4.9 25.3 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 Oct 26 10:32:19 2024

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