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Calcium in PDB 2zyh: Mutant A. Fulgidus Lipase S136A Complexed with Fatty Acid Fragment

Enzymatic activity of Mutant A. Fulgidus Lipase S136A Complexed with Fatty Acid Fragment

All present enzymatic activity of Mutant A. Fulgidus Lipase S136A Complexed with Fatty Acid Fragment:
3.1.1.3;

Protein crystallography data

The structure of Mutant A. Fulgidus Lipase S136A Complexed with Fatty Acid Fragment, PDB code: 2zyh was solved by C.K.Chen, T.P.Ko, R.T.Guo, A.H.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.83
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 91.196, 107.873, 118.896, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 22.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Mutant A. Fulgidus Lipase S136A Complexed with Fatty Acid Fragment (pdb code 2zyh). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Mutant A. Fulgidus Lipase S136A Complexed with Fatty Acid Fragment, PDB code: 2zyh:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2zyh

Go back to Calcium Binding Sites List in 2zyh
Calcium binding site 1 out of 2 in the Mutant A. Fulgidus Lipase S136A Complexed with Fatty Acid Fragment


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Mutant A. Fulgidus Lipase S136A Complexed with Fatty Acid Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca700

b:20.7
occ:1.00
OD1 A:ASP405 2.2 17.3 1.0
O A:LYS411 2.4 20.8 1.0
O A:ARG406 2.5 20.5 1.0
OD1 A:ASP431 2.5 18.4 1.0
OD2 A:ASP409 2.5 26.2 1.0
O A:HOH476 2.6 26.3 1.0
OD2 A:ASP431 2.7 22.6 1.0
CG A:ASP431 3.0 21.1 1.0
CG A:ASP405 3.5 16.3 1.0
CG A:ASP409 3.6 27.9 1.0
C A:LYS411 3.6 21.0 1.0
C A:ARG406 3.6 22.1 1.0
N A:ARG406 3.8 20.6 1.0
OD1 A:ASP409 3.9 28.6 1.0
C A:ASP405 4.0 18.1 1.0
N A:LYS411 4.1 18.3 1.0
CA A:ARG406 4.2 21.4 1.0
OD2 A:ASP405 4.3 19.6 1.0
CA A:LYS411 4.3 20.9 1.0
CA A:ASP405 4.4 17.3 1.0
NE A:ARG406 4.4 24.9 1.0
CB A:ARG406 4.5 20.1 1.0
CB A:ASP431 4.5 18.4 1.0
CB A:ASP405 4.5 18.1 1.0
CB A:LYS411 4.6 24.4 1.0
O A:ASP405 4.6 18.7 1.0
N A:SER412 4.6 19.8 1.0
N A:ASP409 4.7 23.4 1.0
N A:ASP413 4.7 25.9 1.0
N A:GLY407 4.7 22.1 1.0
OD2 A:ASP413 4.8 38.2 1.0
CA A:SER412 4.9 20.2 1.0
CD A:ARG406 4.9 24.8 1.0
CB A:ASP409 4.9 26.1 1.0
N A:ALA408 5.0 23.7 1.0

Calcium binding site 2 out of 2 in 2zyh

Go back to Calcium Binding Sites List in 2zyh
Calcium binding site 2 out of 2 in the Mutant A. Fulgidus Lipase S136A Complexed with Fatty Acid Fragment


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Mutant A. Fulgidus Lipase S136A Complexed with Fatty Acid Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca700

b:17.4
occ:1.00
O B:ARG406 2.4 15.8 1.0
O B:LYS411 2.4 16.9 1.0
OD1 B:ASP405 2.4 18.0 1.0
O B:HOH907 2.4 22.1 1.0
OD2 B:ASP409 2.5 17.6 1.0
OD1 B:ASP431 2.6 16.3 1.0
OD2 B:ASP431 2.6 19.9 1.0
CG B:ASP431 3.0 13.3 1.0
CG B:ASP409 3.5 20.9 1.0
C B:ARG406 3.6 17.9 1.0
C B:LYS411 3.6 19.3 1.0
CG B:ASP405 3.7 16.9 1.0
N B:ARG406 3.8 17.6 1.0
OD1 B:ASP409 3.9 22.1 1.0
C B:ASP405 4.0 16.0 1.0
N B:LYS411 4.2 18.7 1.0
CA B:ARG406 4.2 16.4 1.0
CA B:LYS411 4.3 18.2 1.0
CA B:ASP405 4.4 16.2 1.0
NE B:ARG406 4.4 20.5 1.0
OD2 B:ASP405 4.5 18.8 1.0
CB B:ASP431 4.5 15.3 1.0
CB B:ARG406 4.5 17.7 1.0
OD2 B:ASP413 4.5 39.4 1.0
CB B:LYS411 4.6 20.3 1.0
O B:ASP405 4.6 17.6 1.0
N B:SER412 4.6 19.2 1.0
CB B:ASP405 4.6 16.6 1.0
N B:GLY407 4.7 18.6 1.0
N B:ASP413 4.7 24.1 1.0
N B:ASP409 4.7 20.4 1.0
CA B:SER412 4.8 21.1 1.0
N B:ALA408 4.9 20.0 1.0
CA B:GLY407 4.9 20.6 1.0
CB B:ASP409 4.9 21.9 1.0

Reference:

C.K.Chen, G.C.Lee, T.P.Ko, R.T.Guo, L.M.Huang, H.J.Liu, Y.F.Ho, J.F.Shaw, A.H.Wang. Structure of the Alkalohyperthermophilic Archaeoglobus Fulgidus Lipase Contains A Unique C-Terminal Domain Essential For Long-Chain Substrate Binding. J.Mol.Biol. V. 390 672 2009.
ISSN: ISSN 0022-2836
PubMed: 19447113
DOI: 10.1016/J.JMB.2009.05.017
Page generated: Sat Dec 12 04:02:16 2020

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