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Calcium in PDB 1zl7: Crystal Structure of Catalytically-Active Phospholipase A2 with Bound Calcium

Enzymatic activity of Crystal Structure of Catalytically-Active Phospholipase A2 with Bound Calcium

All present enzymatic activity of Crystal Structure of Catalytically-Active Phospholipase A2 with Bound Calcium:
3.1.1.4;

Protein crystallography data

The structure of Crystal Structure of Catalytically-Active Phospholipase A2 with Bound Calcium, PDB code: 1zl7 was solved by M.T.Murakami, A.C.Cintra, A.Gabdoulkhakov, N.Genov, C.Betzel, R.K.Arni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.90 / 1.60
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 39.206, 53.218, 90.057, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 23.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Catalytically-Active Phospholipase A2 with Bound Calcium (pdb code 1zl7). 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 Catalytically-Active Phospholipase A2 with Bound Calcium, PDB code: 1zl7:

Calcium binding site 1 out of 1 in 1zl7

Go back to Calcium Binding Sites List in 1zl7
Calcium binding site 1 out of 1 in the Crystal Structure of Catalytically-Active Phospholipase A2 with Bound Calcium


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 Catalytically-Active Phospholipase A2 with Bound Calcium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1001

b:33.4
occ:0.60
O A:TYR27 2.3 19.1 1.0
OD1 A:ASP48 2.4 23.9 1.0
N A:GLY32 2.8 22.0 1.0
OD2 A:ASP48 2.8 29.0 1.0
CG A:ASP48 2.8 23.9 1.0
C A:TYR27 3.1 17.2 1.0
N A:GLY31 3.1 24.4 0.5
CD2 A:TYR27 3.1 14.1 1.0
CA A:TYR27 3.2 17.5 1.0
N A:GLY31 3.2 25.0 0.5
C A:LEU30 3.2 25.0 0.5
CB A:TYR27 3.3 16.8 1.0
CA A:LEU30 3.4 23.8 0.5
CA A:GLY32 3.4 20.0 1.0
C A:LEU30 3.5 24.3 0.5
CA A:LEU30 3.5 24.9 0.5
CG A:TYR27 3.7 14.6 1.0
N A:LEU30 3.7 23.3 0.5
O A:LEU30 3.7 25.9 0.5
C A:GLY31 3.8 24.0 1.0
O A:HOH1032 3.8 25.7 1.0
CA A:GLY31 3.9 24.1 1.0
N A:LEU30 3.9 23.7 0.5
CB A:ASP48 4.0 20.2 1.0
O A:CYS44 4.1 17.4 1.0
CE2 A:TYR27 4.2 15.2 1.0
N A:CYS28 4.3 17.1 0.5
N A:CYS28 4.3 16.9 0.5
O A:LEU30 4.4 24.6 0.5
N A:TYR27 4.5 16.7 1.0
C A:GLY29 4.6 23.2 0.5
O A:GLY29 4.6 23.5 0.5
C A:GLY32 4.6 19.2 1.0
O A:CYS26 4.6 16.4 1.0
C A:CYS44 4.7 16.8 1.0
CB A:LEU30 4.8 23.5 0.5
O1 A:GOL1002 4.8 31.1 1.0
O A:CYS28 4.9 20.1 0.5
CB A:CYS44 4.9 17.0 1.0
O A:GLY31 4.9 24.8 1.0
CA A:CYS28 4.9 16.8 0.5
CB A:LEU30 5.0 24.8 0.5
C A:GLY29 5.0 22.9 0.5
C A:CYS28 5.0 18.9 0.5
CA A:CYS28 5.0 16.6 0.5
CD1 A:TYR27 5.0 14.3 1.0

Reference:

M.T.Murakami, A.Gabdoulkhakov, N.Genov, A.C.Cintra, C.Betzel, R.K.Arni. Insights Into Metal Ion Binding in Phospholipases A(2): Ultra High-Resolution Crystal Structures of An Acidic Phospholipase A(2) in the Ca(2+) Free and Bound States. Biochimie V. 88 543 2006.
ISSN: ISSN 0300-9084
PubMed: 16376474
DOI: 10.1016/J.BIOCHI.2005.10.014
Page generated: Sat Dec 12 03:30:15 2020

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