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Calcium in PDB 1qd6: Outer Membrane Phospholipase A From Escherichia Coli

Enzymatic activity of Outer Membrane Phospholipase A From Escherichia Coli

All present enzymatic activity of Outer Membrane Phospholipase A From Escherichia Coli:
3.1.1.32;

Protein crystallography data

The structure of Outer Membrane Phospholipase A From Escherichia Coli, PDB code: 1qd6 was solved by H.J.Snijder, I.Ubarretxena-Belandia, M.Blaauw, K.H.Kalk, H.M.Verheij, M.R.Egmond, N.Dekker, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.30 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 80.067, 84.038, 95.245, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 28.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Outer Membrane Phospholipase A From Escherichia Coli (pdb code 1qd6). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Outer Membrane Phospholipase A From Escherichia Coli, PDB code: 1qd6:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1qd6

Go back to Calcium Binding Sites List in 1qd6
Calcium binding site 1 out of 2 in the Outer Membrane Phospholipase A From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Outer Membrane Phospholipase A From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca1

b:2.3
occ:1.00
O D:SER106 2.4 32.1 1.0
O C:ARG147 2.4 25.9 1.0
O C:HOH294 2.5 45.6 1.0
O D:HOH275 2.5 35.0 1.0
OG C:SER152 2.5 31.2 1.0
O C:HOH285 2.8 27.4 1.0
CB D:SER106 3.5 36.4 1.0
C D:SER106 3.5 32.2 1.0
CB C:SER152 3.6 28.8 1.0
C C:ARG147 3.6 26.9 1.0
N C:ARG147 3.9 23.8 1.0
CA D:SER106 4.1 32.5 1.0
O D:SER107 4.2 27.9 1.0
O2S C:HDS270 4.3 33.9 1.0
CA C:SER152 4.3 25.3 1.0
OG D:SER106 4.4 45.3 1.0
CA C:ARG147 4.4 24.8 1.0
C C:GLY146 4.5 23.7 1.0
C D:SER107 4.5 26.0 1.0
N C:SER148 4.6 25.6 1.0
N D:SER107 4.6 30.4 1.0
OD1 C:ASN145 4.6 19.9 1.0
OD2 C:ASP184 4.7 36.0 1.0
CA C:SER148 4.7 30.4 1.0
CA C:GLY146 4.7 21.2 1.0
N C:GLY146 4.8 21.1 1.0
N C:ARG153 4.9 25.2 1.0
N D:PRO108 5.0 22.6 1.0

Calcium binding site 2 out of 2 in 1qd6

Go back to Calcium Binding Sites List in 1qd6
Calcium binding site 2 out of 2 in the Outer Membrane Phospholipase A From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Outer Membrane Phospholipase A From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca2

b:10.7
occ:1.00
O C:SER106 2.4 33.6 1.0
O D:ARG147 2.4 32.8 1.0
O D:HOH302 2.5 40.7 1.0
OG D:SER152 2.7 37.3 1.0
CB C:SER106 3.4 36.1 1.0
C C:SER106 3.4 31.7 1.0
CB D:SER152 3.6 24.9 1.0
C D:ARG147 3.6 31.1 1.0
CA C:SER106 3.9 32.7 1.0
N D:ARG147 4.0 31.2 1.0
O D:HOH293 4.3 35.4 1.0
O2S D:HDS270 4.3 28.1 1.0
CA D:SER152 4.3 26.6 1.0
O C:SER107 4.4 28.5 1.0
CA D:ARG147 4.4 31.0 1.0
OG C:SER106 4.5 37.1 1.0
C D:GLY146 4.6 28.0 1.0
C C:SER107 4.6 30.6 1.0
N C:SER107 4.6 31.4 1.0
N D:SER148 4.6 32.7 1.0
OD1 D:ASN145 4.6 21.4 1.0
CA D:SER148 4.8 35.3 1.0
OD2 D:ASP184 4.8 43.9 1.0
CA D:GLY146 4.8 28.2 1.0
N D:ARG153 4.9 25.5 1.0
N D:GLY146 4.9 26.6 1.0
N C:PRO108 5.0 31.0 1.0

Reference:

H.J.Snijder, I.Ubarretxena-Belandia, M.Blaauw, K.H.Kalk, H.M.Verheij, M.R.Egmond, N.Dekker, B.W.Dijkstra. Structural Evidence For Dimerization-Regulated Activation of An Integral Membrane Phospholipase. Nature V. 401 717 1999.
ISSN: ISSN 0028-0836
PubMed: 10537112
DOI: 10.1038/44890
Page generated: Thu Jul 11 21:42:24 2024

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