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Calcium in PDB 1uhb: Crystal Structure of Porcine Alpha Trypsin Bound with Auto Catalyticaly Produced Native Peptide at 2.15 A Resolution

Enzymatic activity of Crystal Structure of Porcine Alpha Trypsin Bound with Auto Catalyticaly Produced Native Peptide at 2.15 A Resolution

All present enzymatic activity of Crystal Structure of Porcine Alpha Trypsin Bound with Auto Catalyticaly Produced Native Peptide at 2.15 A Resolution:
3.4.21.4;

Protein crystallography data

The structure of Crystal Structure of Porcine Alpha Trypsin Bound with Auto Catalyticaly Produced Native Peptide at 2.15 A Resolution, PDB code: 1uhb was solved by V.Pattabhi, B.Syed Ibrahim, N.Shamaladevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.31 / 2.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.945, 53.921, 77.245, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 22.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Porcine Alpha Trypsin Bound with Auto Catalyticaly Produced Native Peptide at 2.15 A Resolution (pdb code 1uhb). 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 Porcine Alpha Trypsin Bound with Auto Catalyticaly Produced Native Peptide at 2.15 A Resolution, PDB code: 1uhb:

Calcium binding site 1 out of 1 in 1uhb

Go back to Calcium Binding Sites List in 1uhb
Calcium binding site 1 out of 1 in the Crystal Structure of Porcine Alpha Trypsin Bound with Auto Catalyticaly Produced Native Peptide at 2.15 A Resolution


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 Porcine Alpha Trypsin Bound with Auto Catalyticaly Produced Native Peptide at 2.15 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca256

b:26.5
occ:1.00
 OE1 A:GLU70 2.5 10.8 1.0
O A:VAL75 2.6 18.5 1.0
OE1 A:GLU80 2.7 22.1 1.0
O A:ASN72 2.7 15.6 1.0
OE1 A:GLU77 2.7 23.4 1.0
O A:HOH257 2.7 8.5 1.0
CD A:GLU77 3.4 24.7 1.0
CD A:GLU70 3.5 12.0 1.0
C A:ASN72 3.6 14.0 1.0
CG A:GLU77 3.6 25.3 1.0
CD A:GLU80 3.6 21.7 1.0
C A:VAL75 3.6 17.3 1.0
CG A:GLU80 3.8 20.9 1.0
OE2 A:GLU70 3.8 17.0 1.0
N A:GLU77 3.9 22.0 1.0
N A:ASN72 4.1 12.1 1.0
CA A:LEU76 4.2 20.7 1.0
CB A:GLU77 4.2 24.4 1.0
N A:LEU76 4.3 18.4 1.0
CA A:ASN72 4.3 13.5 1.0
N A:ILE73 4.4 13.6 1.0
N A:VAL75 4.4 16.4 1.0
OE2 A:GLU77 4.4 26.0 1.0
C A:LEU76 4.5 21.6 1.0
CA A:ILE73 4.5 15.1 1.0
N A:HIS71 4.5 12.4 1.0
CB A:ASN72 4.5 11.6 1.0
CA A:VAL75 4.6 16.5 1.0
OE2 A:GLU80 4.7 21.8 1.0
CA A:GLU77 4.8 22.8 1.0
CA A:GLU70 4.8 9.4 1.0
CG A:GLU70 4.8 10.7 1.0
C A:ILE73 4.9 15.9 1.0

Reference:

B.S.Ibrahim, N.Shamaladevi, V.Pattabhi. Trypsin Activity Reduced By An Autocatalytically Produced Nonapeptide. J.Biomol.Struct.Dyn. V. 21 737 2004.
ISSN: ISSN 0739-1102
PubMed: 15106996
DOI: 10.1080/07391102.2004.10506964
Page generated: Thu Jul 11 23:23:44 2024

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