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Calcium in PDB 3wdj: Crystal Structure of Pullulanase Complexed with Maltotetraose From Anoxybacillus Sp. LM18-11

Enzymatic activity of Crystal Structure of Pullulanase Complexed with Maltotetraose From Anoxybacillus Sp. LM18-11

All present enzymatic activity of Crystal Structure of Pullulanase Complexed with Maltotetraose From Anoxybacillus Sp. LM18-11:
3.2.1.41;

Protein crystallography data

The structure of Crystal Structure of Pullulanase Complexed with Maltotetraose From Anoxybacillus Sp. LM18-11, PDB code: 3wdj was solved by J.Xu, F.Ren, C.H.Huang, Y.Zheng, J.Zhen, T.P.Ko, C.C.Chen, H.C.Chan, R.T.Guo, Y.Ma, H.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.22
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 139.971, 65.929, 90.921, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 21.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Pullulanase Complexed with Maltotetraose From Anoxybacillus Sp. LM18-11 (pdb code 3wdj). 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 Pullulanase Complexed with Maltotetraose From Anoxybacillus Sp. LM18-11, PDB code: 3wdj:

Calcium binding site 1 out of 1 in 3wdj

Go back to Calcium Binding Sites List in 3wdj
Calcium binding site 1 out of 1 in the Crystal Structure of Pullulanase Complexed with Maltotetraose From Anoxybacillus Sp. LM18-11


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 Pullulanase Complexed with Maltotetraose From Anoxybacillus Sp. LM18-11 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca805

b:28.2
occ:1.00
 O A:PHE283 2.5 21.2 1.0
OD1 A:ASP282 2.7 22.9 1.0
OE1 A:GLU308 2.7 24.4 1.0
OE2 A:GLU288 2.7 26.9 1.0
O A:HOH1487 2.7 28.7 1.0
O A:HOH1485 2.7 22.3 1.0
O A:HOH1486 2.8 29.3 1.0
OE2 A:GLU308 3.3 25.1 1.0
CD A:GLU308 3.3 24.5 1.0
CD A:GLU288 3.6 28.9 1.0
CG A:ASP282 3.6 21.7 1.0
C A:PHE283 3.6 21.5 1.0
N A:PHE283 3.8 19.6 1.0
CG A:GLU288 3.9 29.6 1.0
O A:HOH919 3.9 19.7 1.0
OD2 A:ASP282 4.0 21.4 1.0
CA A:PHE283 4.3 21.1 1.0
N A:GLY309 4.4 22.4 1.0
OE1 A:GLU288 4.6 25.8 1.0
OE2 A:GLU284 4.6 37.6 1.0
C A:ASP282 4.6 19.8 1.0
O A:VAL286 4.7 27.1 1.0
N A:GLU284 4.7 23.4 1.0
CG A:GLU308 4.7 23.6 1.0
CA A:ASP282 4.8 19.6 1.0
CB A:ASP282 4.8 19.8 1.0
CD1 A:PHE283 4.8 23.2 1.0
CA A:ASN194 4.9 25.7 1.0
CA A:GLU308 4.9 21.7 1.0
CA A:GLU284 4.9 23.9 1.0

Reference:

J.Xu, F.Ren, C.H.Huang, Y.Zheng, J.Zhen, C.C.Chen, H.C.Chan, R.T.Guo, Y.Ma, H.Song. Cloning, Expression, Functional and Structural Studies of Pullulanase From Anoxybacillus Sp. LM18-11 To Be Published.
Page generated: Sat Jul 13 21:00:52 2024

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