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Calcium in PDB 2bd5: Porcine Pancreatic Elastase Complexed with Beta-Casomorphin-7 and Lys- Ser at pH 5 and Immersed in pH 9 Buffer For 30 Seconds

Enzymatic activity of Porcine Pancreatic Elastase Complexed with Beta-Casomorphin-7 and Lys- Ser at pH 5 and Immersed in pH 9 Buffer For 30 Seconds

All present enzymatic activity of Porcine Pancreatic Elastase Complexed with Beta-Casomorphin-7 and Lys- Ser at pH 5 and Immersed in pH 9 Buffer For 30 Seconds:
3.4.21.36;

Protein crystallography data

The structure of Porcine Pancreatic Elastase Complexed with Beta-Casomorphin-7 and Lys- Ser at pH 5 and Immersed in pH 9 Buffer For 30 Seconds, PDB code: 2bd5 was solved by B.Liu, C.J.Schofield, R.C.Wilmouth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.70 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.655, 57.585, 74.524, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 21.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Porcine Pancreatic Elastase Complexed with Beta-Casomorphin-7 and Lys- Ser at pH 5 and Immersed in pH 9 Buffer For 30 Seconds (pdb code 2bd5). 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 Porcine Pancreatic Elastase Complexed with Beta-Casomorphin-7 and Lys- Ser at pH 5 and Immersed in pH 9 Buffer For 30 Seconds, PDB code: 2bd5:

Calcium binding site 1 out of 1 in 2bd5

Go back to Calcium Binding Sites List in 2bd5
Calcium binding site 1 out of 1 in the Porcine Pancreatic Elastase Complexed with Beta-Casomorphin-7 and Lys- Ser at pH 5 and Immersed in pH 9 Buffer For 30 Seconds


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Porcine Pancreatic Elastase Complexed with Beta-Casomorphin-7 and Lys- Ser at pH 5 and Immersed in pH 9 Buffer For 30 Seconds within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca260

b:29.2
occ:1.00
 O A:ASN72 2.3 28.3 1.0
OE1 A:GLU80 2.3 24.6 1.0
O A:HOH378 2.3 37.4 1.0
OE1 A:GLU70 2.3 33.6 1.0
O A:GLN75 2.3 27.9 1.0
ND2 A:ASN77 2.5 29.0 1.0
CD A:GLU70 3.0 31.8 1.0
OE2 A:GLU70 3.0 39.4 1.0
CD A:GLU80 3.4 31.3 1.0
C A:ASN72 3.5 31.5 1.0
C A:GLN75 3.5 33.6 1.0
CG A:ASN77 3.6 31.7 1.0
CG A:GLU80 3.8 32.7 1.0
N A:ASN77 3.9 32.2 1.0
CB A:ASN77 4.1 30.4 1.0
N A:ASN72 4.1 27.9 1.0
N A:GLN75 4.3 31.9 1.0
CA A:ASN72 4.3 27.9 1.0
CA A:ASN76 4.3 31.9 1.0
N A:ASN76 4.3 31.0 1.0
C A:ASN76 4.4 30.7 1.0
O A:HOH395 4.4 42.8 1.0
OE2 A:GLU80 4.4 25.3 1.0
N A:LEU73 4.4 27.4 1.0
C A:LEU73 4.5 33.0 1.0
CG A:GLU70 4.5 24.4 1.0
OD1 A:ASN77 4.5 30.7 1.0
CA A:GLN75 4.5 35.5 1.0
CA A:LEU73 4.5 29.9 1.0
CB A:ASN72 4.6 27.2 1.0
N A:HIS71 4.6 24.0 1.0
O A:LEU73 4.6 35.5 1.0
CA A:ASN77 4.6 32.9 1.0
O A:HOH377 4.8 33.4 1.0
N A:ASN74 4.8 29.9 1.0

Reference:

B.Liu, C.J.Schofield, R.C.Wilmouth. Structural Analyses on Intermediates in Serine Protease Catalysis J.Biol.Chem. V. 281 24024 2006.
ISSN: ISSN 0021-9258
PubMed: 16754679
DOI: 10.1074/JBC.M600495200
Page generated: Fri Jul 12 09:01:15 2024

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