Calcium in PDB 5wzu: Crystal Structure of Human Secreted Phospholipase A2 Group Iie with Compound 24

Enzymatic activity of Crystal Structure of Human Secreted Phospholipase A2 Group Iie with Compound 24

All present enzymatic activity of Crystal Structure of Human Secreted Phospholipase A2 Group Iie with Compound 24:
3.1.1.4;

Protein crystallography data

The structure of Crystal Structure of Human Secreted Phospholipase A2 Group Iie with Compound 24, PDB code: 5wzu was solved by S.Hou, J.Xu, T.Xu, J.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.48 / 2.20
Space group P 21 2 2
Cell size a, b, c (Å), α, β, γ (°) 48.627, 60.469, 63.499, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 23.7

Other elements in 5wzu:

The structure of Crystal Structure of Human Secreted Phospholipase A2 Group Iie with Compound 24 also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Chlorine (Cl) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Human Secreted Phospholipase A2 Group Iie with Compound 24 (pdb code 5wzu). 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 Human Secreted Phospholipase A2 Group Iie with Compound 24, PDB code: 5wzu:

Calcium binding site 1 out of 1 in 5wzu

Go back to Calcium Binding Sites List in 5wzu
Calcium binding site 1 out of 1 in the Crystal Structure of Human Secreted Phospholipase A2 Group Iie with Compound 24


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 Human Secreted Phospholipase A2 Group Iie with Compound 24 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca201

b:48.3
occ:1.00
 O A:TYR26 2.1 22.1 1.0
O A:GLY28 2.3 43.8 1.0
O A:GLY30 2.4 35.3 1.0
OAT A:7W3202 2.5 50.9 1.0
OD1 A:ASP47 2.7 23.1 1.0
OD2 A:ASP47 2.8 24.3 1.0
CG A:ASP47 3.1 22.9 1.0
OAP A:7W3202 3.2 62.0 1.0
C A:TYR26 3.4 22.6 1.0
CAQ A:7W3202 3.5 46.3 1.0
C A:GLY28 3.5 41.8 1.0
C A:GLY30 3.6 39.4 1.0
NAR A:7W3202 3.7 43.3 1.0
N A:GLY28 3.8 31.4 1.0
O A:HOH356 3.9 33.4 1.0
N A:GLY30 3.9 38.4 1.0
OAL A:7W3202 4.0 61.8 1.0
CAN A:7W3202 4.0 72.1 1.0
C A:ILE29 4.1 42.3 1.0
CA A:TYR26 4.2 22.1 1.0
CA A:GLY30 4.2 40.6 1.0
N A:CYS27 4.3 22.1 1.0
C A:CYS27 4.3 27.6 1.0
CA A:CYS27 4.3 23.7 1.0
CA A:GLY28 4.3 37.1 1.0
N A:ILE29 4.4 42.7 1.0
CA A:ILE29 4.5 48.0 1.0
O A:ILE29 4.6 40.2 1.0
N A:GLY31 4.7 40.9 1.0
CB A:ASP47 4.7 20.3 1.0
CB A:TYR26 4.7 22.5 1.0
CAM A:7W3202 4.7 67.3 1.0
CAF A:7W3202 4.7 58.0 1.0
O A:HOH303 4.8 31.8 1.0
O A:CYS43 4.8 20.1 1.0
OAO A:7W3202 4.8 71.1 1.0
CAK A:7W3202 4.9 50.3 1.0
CA A:GLY31 4.9 43.0 1.0

Reference:

S.Hou, T.Xu, J.Xu, L.Qu, Y.Xu, L.Chen, J.Liu. Structural Basis For Functional Selectivity and Ligand Recognition Revealed By Crystal Structures of Human Secreted Phospholipase A2 Group Iie Sci Rep V. 7 10815 2017.
ISSN: ESSN 2045-2322
PubMed: 28883454
DOI: 10.1038/S41598-017-11219-8
Page generated: Sat Dec 12 05:50:14 2020

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