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Arsenic in PDB 5hwa: Crystal Structure of Mh-K1 Chitosanase in Substrate-Bound Form

Enzymatic activity of Crystal Structure of Mh-K1 Chitosanase in Substrate-Bound Form

All present enzymatic activity of Crystal Structure of Mh-K1 Chitosanase in Substrate-Bound Form:
3.2.1.132;

Protein crystallography data

The structure of Crystal Structure of Mh-K1 Chitosanase in Substrate-Bound Form, PDB code: 5hwa was solved by M.Suzuki, A.Saito, A.Ando, K.Miki, J.Saito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.69 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.750, 79.030, 94.760, 90.00, 90.00, 90.00
R / Rfree (%) 13.7 / 17

Other elements in 5hwa:

The structure of Crystal Structure of Mh-K1 Chitosanase in Substrate-Bound Form also contains other interesting chemical elements:

Zinc (Zn) 7 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Mh-K1 Chitosanase in Substrate-Bound Form (pdb code 5hwa). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of Mh-K1 Chitosanase in Substrate-Bound Form, PDB code: 5hwa:

Arsenic binding site 1 out of 1 in 5hwa

Go back to Arsenic Binding Sites List in 5hwa
Arsenic binding site 1 out of 1 in the Crystal Structure of Mh-K1 Chitosanase in Substrate-Bound Form


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Mh-K1 Chitosanase in Substrate-Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As305

b:19.1
occ:0.80
AS A:CAC305 0.0 19.1 0.8
O1 A:CAC305 1.7 21.4 0.8
O2 A:CAC305 1.7 19.7 1.0
C2 A:CAC305 2.0 21.3 0.8
C1 A:CAC305 2.0 26.6 0.8
OXT A:ACY308 2.9 20.0 1.0
ZN A:ZN310 3.2 12.7 0.6
ZN A:ZN309 3.3 21.3 0.9
OD1 A:ASP255 3.5 19.3 1.0
O A:HOH575 3.7 20.2 1.0
O A:HOH617 3.9 41.4 1.0
OE1 A:GLU257 3.9 21.9 1.0
C A:ACY308 4.0 20.0 1.0
O A:ACY307 4.2 26.1 1.0
CH3 A:ACY308 4.5 20.0 1.0
OXT A:ACY307 4.6 35.5 1.0
CG A:ASP255 4.7 20.9 1.0
OXT A:ACY306 4.8 17.9 1.0
O A:HOH545 4.8 23.1 1.0
O A:ACY308 4.9 20.0 1.0
C A:ACY307 4.9 31.1 1.0

Reference:

M.Suzuki, A.Saito, M.Kobayashi, T.Yokoyama, S.Omiya, J.Li, K.Sugita, A.Ando, K.Miki, J.Saito. Understanding For the Catalytic Mechanism Based on the Substrate-Bound Structure of Gh-46 Chitosanase From Bacillus Circulans Mh-K1 To Be Published.
Page generated: Sat Dec 12 01:46:52 2020

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