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Calcium in PDB 1p2i: Structural Consequences of Accommodation of Four Non- Cognate Amino-Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin

Enzymatic activity of Structural Consequences of Accommodation of Four Non- Cognate Amino-Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin

All present enzymatic activity of Structural Consequences of Accommodation of Four Non- Cognate Amino-Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin:
3.4.21.4;

Protein crystallography data

The structure of Structural Consequences of Accommodation of Four Non- Cognate Amino-Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin, PDB code: 1p2i was solved by R.Helland, H.Czapinska, I.Leiros, M.Olufsen, J.Otlewski, A.O.Smalaas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.41 / 1.65
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 74.700, 81.000, 124.090, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 21

Calcium Binding Sites:

The binding sites of Calcium atom in the Structural Consequences of Accommodation of Four Non- Cognate Amino-Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin (pdb code 1p2i). 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 Structural Consequences of Accommodation of Four Non- Cognate Amino-Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin, PDB code: 1p2i:

Calcium binding site 1 out of 1 in 1p2i

Go back to Calcium Binding Sites List in 1p2i
Calcium binding site 1 out of 1 in the Structural Consequences of Accommodation of Four Non- Cognate Amino-Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structural Consequences of Accommodation of Four Non- Cognate Amino-Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca600

b:23.3
occ:1.00
 O A:VAL75 2.2 29.4 1.0
OE2 A:GLU80 2.3 24.9 1.0
OE2 A:GLU70 2.3 19.5 1.0
O A:ASN72 2.3 21.7 1.0
O A:HOH1044 2.4 21.7 1.0
O A:HOH1021 2.4 21.6 1.0
CD A:GLU80 3.3 25.4 1.0
CD A:GLU70 3.3 19.9 1.0
C A:VAL75 3.4 29.6 1.0
C A:ASN72 3.5 22.0 1.0
CG A:GLU80 3.6 26.5 1.0
OE1 A:GLU70 3.7 20.3 1.0
N A:GLU77 4.1 35.6 1.0
CA A:VAL76 4.1 33.2 1.0
CG A:GLU77 4.1 38.2 1.0
N A:VAL76 4.2 31.0 1.0
OE2 A:GLU77 4.2 38.2 1.0
N A:VAL75 4.2 27.0 1.0
CA A:ILE73 4.3 23.6 1.0
N A:ILE73 4.3 22.2 1.0
N A:ASN72 4.3 22.2 1.0
CA A:VAL75 4.4 28.0 1.0
CA A:ASN72 4.4 22.2 1.0
OE1 A:GLU80 4.4 25.8 1.0
C A:VAL76 4.5 34.2 1.0
C A:ILE73 4.5 23.8 1.0
O A:HOH1007 4.6 23.0 1.0
N A:ASP71 4.6 20.8 1.0
CB A:ASN72 4.6 23.1 1.0
CG A:GLU70 4.6 20.8 1.0
CD A:GLU77 4.7 39.1 1.0
CB A:GLU77 4.8 36.9 1.0
O A:HOH1059 4.8 29.9 1.0
CA A:GLU70 4.8 21.1 1.0
O A:ILE73 4.9 22.2 1.0
CB A:GLU70 4.9 21.3 1.0
N A:ASN74 4.9 23.5 1.0

Reference:

R.Helland, H.Czapinska, I.Leiros, M.Olufsen, J.Otlewski, A.O.Smalaas. Structural Consequences of Accommodation of Four Non-Cognate Amino Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin. J.Mol.Biol. V. 333 845 2003.
ISSN: ISSN 0022-2836
PubMed: 14568540
DOI: 10.1016/J.JMB.2003.08.059
Page generated: Mon Jul 7 18:07:35 2025

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